Molecular basis of proteinopathies: Etiopathology of dementia and motor disorders

[1] Abner E.L., Kryscio R.J., Schmitt F.A., Santacruz K.S., Jicha G.A., Lin Y., Neltner J.M., Smith C.D., Van Eldik L.J., Nelson P.T.: “End-stage” neurofibrillary tangle pathology in preclinical Alzheimer’s disease: Fact or fiction? J. Alzheimers Dis., 2011; 25: 445–453 AbnerE.L. KryscioR.J. SchmittF.A. SantacruzK.S. JichaG.A. LinY. NeltnerJ.M. SmithC.D. Van EldikL.J. NelsonP.T. “End-stage” neurofibrillary tangle pathology in preclinical Alzheimer’s disease: Fact or fiction? J. Alzheimers Dis. 2011 25 445 453 10.3233/JAD-2011-101980 Search in Google Scholar

[2] Ahmed T., Van der Jeugd A., Blum D., Galas M.C., D’Hooge R., Buee L., Balschun D.: Cognition and hippocampal synaptic plasticity in mice with a homozygous tau deletion. Neurobiol. Aging, 2014; 35: 2474–2478 AhmedT. Van der JeugdA. BlumD. GalasM.C. D’HoogeR. BueeL. BalschunD. Cognition and hippocampal synaptic plasticity in mice with a homozygous tau deletion Neurobiol. Aging 2014 35 2474 2478 10.1016/j.neurobiolaging.2014.05.005 Search in Google Scholar

[3] Amadoro G., Corsetti V., Ciotti M.T., Florenzano F., Capsoni S., Amato G., Calissano P.: Endogenous Aβ causes cell death via early tau hyperphosphorylation. Neurobiol. Aging, 2011; 32: 969–990 AmadoroG. CorsettiV. CiottiM.T. FlorenzanoF. CapsoniS. AmatoG. CalissanoP. Endogenous Aβ causes cell death via early tau hyperphosphorylation Neurobiol. Aging 2011 32 969 990 10.1016/j.neurobiolaging.2009.06.005 Search in Google Scholar

[4] An W.L., Cowburn R.F., Li L., Braak H., Alafuzoff I., Iqbal K., Iqbal I.G., Winblad B., Pei J.J.: Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer’s disease. Am. J. Pathol., 2003; 163: 591–607 AnW.L. CowburnR.F. LiL. BraakH. AlafuzoffI. IqbalK. IqbalI.G. WinbladB. PeiJ.J. Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer’s disease Am. J. Pathol. 2003 163 591 607 10.1016/S0002-9440(10)63687-5 Search in Google Scholar

[5] Arun P., Oguntayo S., Albert S.V., Gist I., Wang Y., Nambiar M.P., Long J.B.: Acute decrease in alkaline phosphatase after brain injury: A potential mechanism for tauopathy. Neurosci. Lett., 2015; 609: 152–158 ArunP. OguntayoS. AlbertS.V. GistI. WangY. NambiarM.P. LongJ.B. Acute decrease in alkaline phosphatase after brain injury: A potential mechanism for tauopathy Neurosci. Lett. 2015 609 152 158 10.1016/j.neulet.2015.10.03626483321 Search in Google Scholar

[6] Avila J., Jiménez J.S., Sayas C.L., Bolós M., Zabala J.C., Rivas G., Hernández F.: Tau structures. Front. Aging Neurosci., 2016; 8: 262 AvilaJ. JiménezJ.S. SayasC.L. BolósM. ZabalaJ.C. RivasG. HernándezF. Tau structures Front. Aging Neurosci. 2016 8 262 10.3389/fnagi.2016.00262509915927877124 Search in Google Scholar

[7] Ayala Y.M., Zago P., D’Ambrogio A., Xu Y.F., Petrucelli L., Buratti E., Baralle F.E.: Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci., 2008; 121: 3778–3785 AyalaY.M. ZagoP. D’AmbrogioA. XuY.F. PetrucelliL. BurattiE. BaralleF.E. Structural determinants of the cellular localization and shuttling of TDP-43 J. Cell Sci. 2008 121 3778 3785 10.1242/jcs.03895018957508 Search in Google Scholar

[8] Bartels T., Choi J.G., Selkoe D.J.: α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature, 2011; 477: 107–110 BartelsT. ChoiJ.G. SelkoeD.J. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation Nature 2011 477 107 110 10.1038/nature10324316636621841800 Search in Google Scholar

[9] Berning B.A., Walker A.K.: The pathobiology of TDP-43 C-terminal fragments in ALS and FTLD. Front. Neurosci., 2019; 13: 335 BerningB.A. WalkerA.K. The pathobiology of TDP-43 C-terminal fragments in ALS and FTLD Front. Neurosci. 2019 13 335 10.3389/fnins.2019.00335647028231031584 Search in Google Scholar

[10] Brandt R., Léger J., Lee G.: Interaction of tau with the neural plasma membrane mediated by tau’s aminoterminal projection domain. J. Cell Biol., 1995; 131: 1327–1340 BrandtR. LégerJ. LeeG. Interaction of tau with the neural plasma membrane mediated by tau’s aminoterminal projection domain J. Cell Biol. 1995 131 1327 1340 10.1083/jcb.131.5.132721206458522593 Search in Google Scholar

[11] Burré J., Sharma M., Südhof T.C.: α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation. Proc. Natl. Acad. Sci. USA, 2014; 111: E4274–E4283 BurréJ. SharmaM. SüdhofT.C. α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation Proc. Natl. Acad. Sci. USA 2014 111 E4274 E4283 10.1073/pnas.1416598111 Search in Google Scholar

[12] Bussell R.Jr., Eliezer D.: Effects of Parkinson’s disease-linked mutations on the structure of lipid-associated α-synuclein. Biochemistry, 2004; 43: 4810–4818 BussellR.Jr. EliezerD. Effects of Parkinson’s disease-linked mutations on the structure of lipid-associated α-synuclein Biochemistry 2004 43 4810 4818 10.1021/bi036135+ Search in Google Scholar

[13] Chartier-Harlin M.C., Kachergus J., Roumier C., Mouroux V., Douay X., Lincoln S., Levecque C., Larvor L., Andrieux J., Hulihan M., Waucquier N., Defebvre L., Amouyel P., Farrer M., Destée A.: α-synuclein locus duplication as a cause of familial Parkinson’s disease. Lancet, 2004; 364: 1167–1169 Chartier-HarlinM.C. KachergusJ. RoumierC. MourouxV. DouayX. LincolnS. LevecqueC. LarvorL. AndrieuxJ. HulihanM. WaucquierN. DefebvreL. AmouyelP. FarrerM. DestéeA. α-synuclein locus duplication as a cause of familial Parkinson’s disease Lancet 2004 364 1167 1169 10.1016/S0140-6736(04)17103-1 Search in Google Scholar

[14] Chen R.H., Wislet-Gendebien S., Samuel F., Visanji N.P., Zhang G., Marsilio D., Langman T., Fraser P.E., Tandon A.: α-Synuclein membrane association is regulated by the Rab3a recycling machinery and presynaptic activity. J. Biol. Chem., 2013; 288: 7438–7449 ChenR.H. Wislet-GendebienS. SamuelF. VisanjiN.P. ZhangG. MarsilioD. LangmanT. FraserP.E. TandonA. α-Synuclein membrane association is regulated by the Rab3a recycling machinery and presynaptic activity J. Biol. Chem. 2013 288 7438 7449 10.1074/jbc.M112.439497359778523344955 Search in Google Scholar

[15] Cherry J.D., Tripodis Y., Alvarez V.E., Huber B., Kiernan P.T., Daneshvar D.H., Mez J., Montenigro P.H., Solomon T.M., Alosco M.L., Stern R.A., McKee A.C., Stein T.D.: Microglial neuroinflammation contributes to tau accumulation in chronic traumatic encephalopathy. Acta Neuropathol. Commun., 2016; 4: 112 CherryJ.D. TripodisY. AlvarezV.E. HuberB. KiernanP.T. DaneshvarD.H. MezJ. MontenigroP.H. SolomonT.M. AloscoM.L. SternR.A. McKeeA.C. SteinT.D. Microglial neuroinflammation contributes to tau accumulation in chronic traumatic encephalopathy Acta Neuropathol. Commun. 2016 4 112 10.1186/s40478-016-0382-8508433327793189 Search in Google Scholar

[16] Chiang C.H., Grauffel C., Wu L.S., Kuo P.H., Doudeva L.G., Lim C., Shen C.K., Yuan H.S.: Structural analysis of disease-related TDP-43 D169G mutation: Linking enhanced stability and caspase cleavage efficiency to protein accumulation. Sci. Rep., 2016; 6: 21581 ChiangC.H. GrauffelC. WuL.S. KuoP.H. DoudevaL.G. LimC. ShenC.K. YuanH.S. Structural analysis of disease-related TDP-43 D169G mutation: Linking enhanced stability and caspase cleavage efficiency to protein accumulation Sci. Rep. 2016 6 21581 10.1038/srep21581475669326883171 Search in Google Scholar

[17] Choi B.K., Choi M.G., Kim J.Y., Yang Y., Lai Y., Kweon D.H., Lee N.K., Shin Y.K.: Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking. Proc. Natl. Acad. Sci. USA, 2013; 110: 4087–4092 ChoiB.K. ChoiM.G. KimJ.Y. YangY. LaiY. KweonD.H. LeeN.K. ShinY.K. Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking Proc. Natl. Acad. Sci. USA 2013 110 4087 4092 10.1073/pnas.1218424110359392523431141 Search in Google Scholar

[18] Clavaguera F., Bolmont T., Crowther R.A., Abramowski D., Frank S., Probst A., Fraser G., Stalder A.K., Beibel M., Staufenbiel M., Jucker M., Goedert M., Tolnay M.: Transmission and spreading of tauopathy in transgenic mouse brain. Nat. Cell Biol., 2009; 11: 909–913 ClavagueraF. BolmontT. CrowtherR.A. AbramowskiD. FrankS. ProbstA. FraserG. StalderA.K. BeibelM. StaufenbielM. JuckerM. GoedertM. TolnayM. Transmission and spreading of tauopathy in transgenic mouse brain Nat. Cell Biol. 2009 11 909 913 10.1038/ncb1901272696119503072 Search in Google Scholar

[19] Cohen T.J., Hwang A.W., Restrepo C.R., Yuan C.X., Trojanowski J.Q., Lee V.M.: An acetylation switch controls TDP-43 function and aggregation propensity. Nat. Commun., 2015; 6: 5845 CohenT.J. HwangA.W. RestrepoC.R. YuanC.X. TrojanowskiJ.Q. LeeV.M. An acetylation switch controls TDP-43 function and aggregation propensity Nat. Commun. 2015 6 5845 10.1038/ncomms6845440736525556531 Search in Google Scholar

[20] Conway K.A., Harper J.D., Lansbury P.T.: Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nat. Med., 1998; 4: 1318–1320 ConwayK.A. HarperJ.D. LansburyP.T. Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease Nat. Med. 1998 4 1318 1320 10.1038/33119809558 Search in Google Scholar

[21] Coskuner O., Wise-Scira O.: Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics. ACS Chem. Neurosci., 2013; 4: 1101–1113 CoskunerO. Wise-SciraO. Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics ACS Chem. Neurosci. 2013 4 1101 1113 10.1021/cn400041j Search in Google Scholar

[22] Dawson H.N., Ferreira A., Eyster M.V., Ghoshal N., Binder L.I., Vitek M.P.: Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci., 2001; 114: 1179–1187 DawsonH.N. FerreiraA. EysterM.V. GhoshalN. BinderL.I. VitekM.P. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice J. Cell Sci. 2001 114 1179 1187 10.1242/jcs.114.6.1179 Search in Google Scholar

[23] Dayanandan R., Van Slegtenhorst M., Mack T.G., Ko L., Yen S.H., Leroy K., Brion J.P., Anderton B.H., Hutton M., Lovestone S.: Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation. FEBS Lett., 1999; 446: 228–232 DayanandanR. Van SlegtenhorstM. MackT.G. KoL. YenS.H. LeroyK. BrionJ.P. AndertonB.H. HuttonM. LovestoneS. Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation FEBS Lett. 1999 446 228 232 10.1016/S0014-5793(99)00222-7 Search in Google Scholar

[24] Dementia. https://www.who.int/en/news-room/fact-sheets/detail/dementia (17.04.2020) Dementia https://www.who.int/en/news-room/fact-sheets/detail/dementia (17.04.2020) Search in Google Scholar

[25] Derisbourg M., Leghay C., Chiappetta G., Fernandez-Gomez F.J., Laurent C., Demeyer D., Carrier S., Buée-Scherrer V., Blum D., Vinh J., Sergeant N., Verdier Y., Buée L., Hamdane M.: Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms. Sci. Rep., 2015; 5: 9659 DerisbourgM. LeghayC. ChiappettaG. Fernandez-GomezF.J. LaurentC. DemeyerD. CarrierS. Buée-ScherrerV. BlumD. VinhJ. SergeantN. VerdierY. BuéeL. HamdaneM. Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms Sci. Rep. 2015 5 9659 10.1038/srep09659443147525974414 Search in Google Scholar

[26] Derkinderen P., Scales T.M., Hanger D.P., Leung K.Y., Byers H.L., Ward M.A., Lenz C., Price C., Bird I.N., Perera T., Kellie S., Williamson R., Noble W., Van Etten R.A., Leroy K. i wsp.: Tyrosine 394 is phosphorylated in Alzheimer’s paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. J. Neurosci., 2005; 25: 6584–6593 DerkinderenP. ScalesT.M. HangerD.P. LeungK.Y. ByersH.L. WardM.A. LenzC. PriceC. BirdI.N. PereraT. KellieS. WilliamsonR. NobleW. Van EttenR.A. LeroyK. Tyrosine 394 is phosphorylated in Alzheimer’s paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase J. Neurosci. 2005 25 6584 6593 10.1523/JNEUROSCI.1487-05.2005672543016014719 Search in Google Scholar

[27] Dixit R., Ross J.L., Goldman Y.E., Holzbaur E.L.: Differential regulation of dynein and kinesin motor proteins by tau. Science, 2008; 319: 1086–1089 DixitR. RossJ.L. GoldmanY.E. HolzbaurE.L. Differential regulation of dynein and kinesin motor proteins by tau Science 2008 319 1086 1089 10.1126/science.1152993286619318202255 Search in Google Scholar

[28] Doherty C.P.A., Ulamec S.M., Maya-Martinez R., Good S.C., Makepeace J., Khan G.N., van Oosten-Hawle P., Radford S.E., Brockwell D.J.: A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function. Nat. Struct. Mol. Biol., 2020; 27: 249–259 DohertyC.P.A. UlamecS.M. Maya-MartinezR. GoodS.C. MakepeaceJ. KhanG.N. van Oosten-HawleP. RadfordS.E. BrockwellD.J. A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function Nat. Struct. Mol. Biol. 2020 27 249 259 10.1038/s41594-020-0384-x710061232157247 Search in Google Scholar

[29] Dugger B.N., Dickson D.W.: Pathology of neurodegenerative diseases. Cold Spring Harb. Perspect. Biol., 2017; 9: a028035 DuggerB.N. DicksonD.W. Pathology of neurodegenerative diseases Cold Spring Harb. Perspect. Biol. 2017 9 a028035 10.1101/cshperspect.a028035549506028062563 Search in Google Scholar

[30] Fares M.B., Ait-Bouziad N., Dikiy I., Mbefo M.K., Jovičić A., Kiely A., Holton J.L., Lee S.J., Gitler A.D., Eliezer D., Lashuel H.A.: The novel Parkinson’s disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells. Hum. Mol. Genet., 2014; 23: 4491–4509 FaresM.B. Ait-BouziadN. DikiyI. MbefoM.K. JovičićA. KielyA. HoltonJ.L. LeeS.J. GitlerA.D. EliezerD. LashuelH.A. The novel Parkinson’s disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells Hum. Mol. Genet. 2014 23 4491 4509 10.1093/hmg/ddu165411940424728187 Search in Google Scholar

[31] Fischer D., Mukrasch M.D., Biernat J., Bibow S., Blackledge M., Griesinger C., Mandelkow E., Zweckstetter M.: Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules. Biochemistry, 2009; 48: 10047–10055 FischerD. MukraschM.D. BiernatJ. BibowS. BlackledgeM. GriesingerC. MandelkowE. ZweckstetterM. Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules Biochemistry 2009 48 10047 10055 10.1021/bi901090m19769346 Search in Google Scholar

[32] Flores B.N., Li X., Malik A.M., Martinez J., Beg A.A., Barmada S.J.: An intramolecular salt bridge linking TDP43 RNA binding, protein stability, and TDP43-dependent neurodegeneration. Cell. Rep., 2019; 27: 1133–1150.e8 FloresB.N. LiX. MalikA.M. MartinezJ. BegA.A. BarmadaS.J. An intramolecular salt bridge linking TDP43 RNA binding, protein stability, and TDP43-dependent neurodegeneration Cell. Rep. 2019 27 1133 1150.e8 10.1016/j.celrep.2019.03.093 Search in Google Scholar

[33] François-Moutal L., Perez-Miller S., Scott D.D., Miranda V.G., Mollasalehi N., Khanna M.: Structural insights into TDP-43 and effects of post-translational modifications. Front. Mol. Neurosci., 2019; 12: 301 François-MoutalL. Perez-MillerS. ScottD.D. MirandaV.G. MollasalehiN. KhannaM. Structural insights into TDP-43 and effects of post-translational modifications Front. Mol. Neurosci. 2019 12 301 10.3389/fnmol.2019.00301 Search in Google Scholar

[34] Fraser P.E., Yang D.S., Yu G., Lévesque L., Nishimura M., Arawaka S., Serpell L.C., Rogaeva E., St George-Hyslop P.: Presenilin structure, function and role in Alzheimer disease. Biochim. Biophys. Acta, 2000; 1502: 1–15 FraserP.E. YangD.S. YuG. LévesqueL. NishimuraM. ArawakaS. SerpellL.C. RogaevaE. St George-HyslopP. Presenilin structure, function and role in Alzheimer disease Biochim. Biophys. Acta 2000 1502 1 15 10.1016/S0925-4439(00)00028-4 Search in Google Scholar

[35] Frenkel-Pinter M., Stempler S., Tal-Mazaki S., Losev Y., Singh-Anand A., Escobar-Álvarez D., Lezmy J., Gazit E., Ruppin E., Segal D.: Altered protein glycosylation predicts Alzheimer’s disease and modulates its pathology in disease model Drosophila. Neurobiol. Aging, 2017; 56: 159–171 Frenkel-PinterM. StemplerS. Tal-MazakiS. LosevY. Singh-AnandA. Escobar-ÁlvarezD. LezmyJ. GazitE. RuppinE. SegalD. Altered protein glycosylation predicts Alzheimer’s disease and modulates its pathology in disease model Drosophila Neurobiol. Aging 2017 56 159 171 10.1016/j.neurobiolaging.2017.04.02028552182 Search in Google Scholar

[36] Fusco G., Chen S.W., Williamson P.T.F., Cascella R., Perni M., Jarvis J.A., Cecchi C., Vendruscolo M., Chiti F., Cremades N., Ying L., Dobson C.M., De Simone A.: Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science, 2017; 358: 1440–1443 FuscoG. ChenS.W. WilliamsonP.T.F. CascellaR. PerniM. JarvisJ.A. CecchiC. VendruscoloM. ChitiF. CremadesN. YingL. DobsonC.M. De SimoneA. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers Science 2017 358 1440 1443 10.1126/science.aan616029242346 Search in Google Scholar

[37] Gámez-Valero A., Beyer K.: Alternative Splicing of alpha- and beta-synuclein genes plays differential roles in synucleinopathies. Genes, 2018; 9: 63 Gámez-ValeroA. BeyerK. Alternative Splicing of alpha- and beta-synuclein genes plays differential roles in synucleinopathies Genes 2018 9 63 10.3390/genes9020063585255929370097 Search in Google Scholar

[38] Garnier C., Devred F., Byrne D., Puppo R., Roman A.Y., Malesinski S., Golovin A.V., Lebrun R., Ninkina N.N., Tsvetkov P.O.: Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates. Sci. Rep., 2017; 7: 6812 GarnierC. DevredF. ByrneD. PuppoR. RomanA.Y. MalesinskiS. GolovinA.V. LebrunR. NinkinaN.N. TsvetkovP.O. Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates Sci. Rep. 2017 7 6812 10.1038/s41598-017-07215-7553373028754988 Search in Google Scholar

[39] Gauthier-Kemper A., Suárez Alonso M., Sündermann F., Niewidok B., Fernandez M.P., Bakota L., Heinisch J.J., Brandt R.: Annexins A2 and A6 interact with the extreme N terminus of tau and thereby contribute to tau’s axonal localization. J. Biol. Chem., 2018; 293: 8065–8076 Gauthier-KemperA. Suárez AlonsoM. SündermannF. NiewidokB. FernandezM.P. BakotaL. HeinischJ.J. BrandtR. Annexins A2 and A6 interact with the extreme N terminus of tau and thereby contribute to tau’s axonal localization J. Biol. Chem. 2018 293 8065 8076 10.1074/jbc.RA117.000490597144629636414 Search in Google Scholar

[40] Gong C.X., Singh T.J., Grundke-Iqbal I., Iqbal K.: Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem., 1993; 61: 921–927 GongC.X. SinghT.J. Grundke-IqbalI. IqbalK. Phosphoprotein phosphatase activities in Alzheimer disease brain J. Neurochem. 1993 61 921 927 10.1111/j.1471-4159.1993.tb03603.x8395566 Search in Google Scholar

[41] Götz J., Probst A., Spillantini M.G., Schäfer T., Jakes R., Bürki K., Goedert M.: Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J., 1995; 14: 1304–1313 GötzJ. ProbstA. SpillantiniM.G. SchäferT. JakesR. BürkiK. GoedertM. Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform EMBO J. 1995 14 1304 1313 10.1002/j.1460-2075.1995.tb07116.x3982157729409 Search in Google Scholar

[42] Gómez-Santos C., Ferrer I., Reiriz J., Viñals F., Barrachina M., Ambrosio S.: MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells. Brain Res., 2002; 935: 32–39 Gómez-SantosC. FerrerI. ReirizJ. ViñalsF. BarrachinaM. AmbrosioS. MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells Brain Res. 2002 935 32 39 10.1016/S0006-8993(02)02422-8 Search in Google Scholar

[43] Hans F., Eckert M., von Zweydorf F., Gloeckner C.J., Kahle P.J.: Identification and characterization of ubiquitinylation sites in TAR DNA-binding protein of 43 kDa (TDP-43). J. Biol. Chem., 2018; 293: 16083–16099 HansF. EckertM. von ZweydorfF. GloecknerC.J. KahleP.J. Identification and characterization of ubiquitinylation sites in TAR DNA-binding protein of 43 kDa (TDP-43) J. Biol. Chem. 2018 293 16083 16099 10.1074/jbc.RA118.003440618762430120199 Search in Google Scholar

[44] Heicklen-Klein A., Ginzburg I.: Tau promoter confers neuronal specificity and binds Sp1 and AP-2. J. Neurochem., 2000; 75: 1408–1418 Heicklen-KleinA. GinzburgI. Tau promoter confers neuronal specificity and binds Sp1 and AP-2 J. Neurochem. 2000 75 1408 1418 10.1046/j.1471-4159.2000.0751408.x10987820 Search in Google Scholar

[45] Highley J.R., Kirby J., Jansweijer J.A., Webb P.S., Hewamadduma C.A., Heath P.R., Higginbottom A., Raman R., Ferraiuolo L., Cooper-Knock J., McDermott C.J., Wharton S.B., Shaw P.J., Ince P.G.: Loss of nuclear TDP-43 in amyotrophic lateral sclerosis (ALS) causes altered expression of splicing machinery and widespread dysregulation of RNA splicing in motor neurones. Neuropathol. Appl. Neurobiol., 2014; 40: 670–685 HighleyJ.R. KirbyJ. JansweijerJ.A. WebbP.S. HewamaddumaC.A. HeathP.R. HigginbottomA. RamanR. FerraiuoloL. Cooper-KnockJ. McDermottC.J. WhartonS.B. ShawP.J. InceP.G. Loss of nuclear TDP-43 in amyotrophic lateral sclerosis (ALS) causes altered expression of splicing machinery and widespread dysregulation of RNA splicing in motor neurones Neuropathol. Appl. Neurobiol. 2014 40 670 685 10.1111/nan.1214824750229 Search in Google Scholar

[46] Hirokawa N., Shiomura Y., Okabe S.: Tau proteins: the molecular structure and mode of binding on microtubules. J. Cell Biol., 1988; 107: 1449–1459 HirokawaN. ShiomuraY. OkabeS. Tau proteins: the molecular structure and mode of binding on microtubules J. Cell Biol. 1988 107 1449 1459 10.1083/jcb.107.4.144921152623139677 Search in Google Scholar

[47] Hosokawa M., Kondo H., Serrano G.E., Beach T.G., Robinson A.C., Mann D.M., Akiyama H., Hasegawa M., Arai T.: Accumulation of multiple neurodegenerative disease-related proteins in familial fronto-temporal lobar degeneration associated with granulin mutation. Sci. Rep., 2017; 7: 1513 HosokawaM. KondoH. SerranoG.E. BeachT.G. RobinsonA.C. MannD.M. AkiyamaH. HasegawaM. AraiT. Accumulation of multiple neurodegenerative disease-related proteins in familial fronto-temporal lobar degeneration associated with granulin mutation Sci. Rep. 2017 7 1513 10.1038/s41598-017-01587-6543143028473694 Search in Google Scholar

[48] Huin V., Buée L., Behal H., Labreuche J., Sablonnière B., Dhaenens C.M.: Alternative promoter usage generates novel shorter MAPT mRNA transcripts in Alzheimer’s disease and progressive supranuclear palsy brains. Sci. Rep., 2017; 7: 12589 HuinV. BuéeL. BehalH. LabreucheJ. SablonnièreB. DhaenensC.M. Alternative promoter usage generates novel shorter MAPT mRNA transcripts in Alzheimer’s disease and progressive supranuclear palsy brains Sci. Rep. 2017 7 12589 10.1038/s41598-017-12955-7562670928974731 Search in Google Scholar

[49] Iguchi Y., Katsuno M., Ikenaka K., Ishigaki S., Sobue G.: Amyotrophic lateral sclerosis: An update on recent genetic insights. J Neurol., 2013; 260: 2917–2927 IguchiY. KatsunoM. IkenakaK. IshigakiS. SobueG. Amyotrophic lateral sclerosis: An update on recent genetic insights J Neurol. 2013 260 2917 2927 10.1007/s00415-013-7112-y24085347 Search in Google Scholar

[50] Ittner L.M., Götz J.: Amyloid-β and tau – a toxic pas de deux in Alzheimer’s disease. Nat. Rev. Neurosci., 2011; 12: 65–72 IttnerL.M. GötzJ. Amyloid-β and tau – a toxic pas de deux in Alzheimer’s disease Nat. Rev. Neurosci. 2011 12 65 72 10.1038/nrn296721193853 Search in Google Scholar

[51] Ittner L.M., Ke Y.D., Delerue F., Bi M., Gladbach A., van Eersel J., Wölfing H., Chieng B.C., Christie M.J., Napier I.A., Eckert A., Staufenbiel M., Hardeman E., Götz J.: Dendritic function of tau mediates amyloid-β toxicity in Alzheimer’s disease mouse models. Cell, 2010; 142: 387–397 IttnerL.M. KeY.D. DelerueF. BiM. GladbachA. van EerselJ. WölfingH. ChiengB.C. ChristieM.J. NapierI.A. EckertA. StaufenbielM. HardemanE. GötzJ. Dendritic function of tau mediates amyloid-β toxicity in Alzheimer’s disease mouse models Cell 2010 142 387 397 10.1016/j.cell.2010.06.03620655099 Search in Google Scholar

[52] Jakes R., Spillantini M.G., Goedert M.: Identification of two distinct synucleins from human brain. FEBS Lett., 1994; 345: 27–32 JakesR. SpillantiniM.G. GoedertM. Identification of two distinct synucleins from human brain FEBS Lett. 1994 345 27 32 10.1016/0014-5793(94)00395-5 Search in Google Scholar

[53] Jao C.C., Der-Sarkissian A., Chen J., Langen R.: Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc. Natl. Acad. Sci. USA, 2004; 101: 8331–8336 JaoC.C. Der-SarkissianA. ChenJ. LangenR. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling Proc. Natl. Acad. Sci. USA 2004 101 8331 8336 10.1073/pnas.040055310142039415155902 Search in Google Scholar

[54] Jiang L.L., Xue W., Hong J.Y., Zhang J.T., Li M.J., Yu S.N., He J.H., Hu H.Y.: The N-terminal dimerization is required for TDP-43 splicing activity. Sci. Rep., 2017; 7: 6196 JiangL.L. XueW. HongJ.Y. ZhangJ.T. LiM.J. YuS.N. HeJ.H. HuH.Y. The N-terminal dimerization is required for TDP-43 splicing activity Sci. Rep. 2017 7 6196 10.1038/s41598-017-06263-3552244628733604 Search in Google Scholar

[55] Jin H., Kanthasamy A., Ghosh A., Yang Y., Anantharam V., Kanthasamy A.G.: α-Synuclein negatively regulates protein kinase Cδ expression to suppress apoptosis in dopaminergic neurons by reducing p300 histone acetyltransferase activity. J. Neurosci., 2011; 31: 2035–2051 JinH. KanthasamyA. GhoshA. YangY. AnantharamV. KanthasamyA.G. α-Synuclein negatively regulates protein kinase Cδ expression to suppress apoptosis in dopaminergic neurons by reducing p300 histone acetyltransferase activity J. Neurosci. 2011 31 2035 2051 10.1523/JNEUROSCI.5634-10.2011304164221307242 Search in Google Scholar

[56] Johnson G.V., Seubert P., Cox T.M., Motter R., Brown J.P., Galasko D.: The tau protein in human cerebrospinal fluid in Alzheimer’s disease consists of proteolytically derived fragments. J. Neurochem., 1997; 68: 430–433 JohnsonG.V. SeubertP. CoxT.M. MotterR. BrownJ.P. GalaskoD. The tau protein in human cerebrospinal fluid in Alzheimer’s disease consists of proteolytically derived fragments J. Neurochem. 1997 68 430 433 10.1046/j.1471-4159.1997.68010430.x8978756 Search in Google Scholar

[57] Kametani F., Nonaka T., Suzuki T., Arai T., Dohmae N., Akiyama H., Hasegawa M.: Identification of casein kinase-1 phosphorylation sites on TDP-43. Biochem. Biophys. Res. Commun., 2009; 382: 405–409 KametaniF. NonakaT. SuzukiT. AraiT. DohmaeN. AkiyamaH. HasegawaM. Identification of casein kinase-1 phosphorylation sites on TDP-43 Biochem. Biophys. Res. Commun. 2009 382 405 409 10.1016/j.bbrc.2009.03.03819285963 Search in Google Scholar

[58] Kanaan N.M., Morfini G.A., LaPointe N.E., Pigino G.F., Patterson K.R., Song Y., Andreadis A., Fu Y., Brady S.T., Binder L.I.: Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J. Neurosci., 2011; 31: 9858–9868 KanaanN.M. MorfiniG.A. LaPointeN.E. PiginoG.F. PattersonK.R. SongY. AndreadisA. FuY. BradyS.T. BinderL.I. Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases J. Neurosci. 2011 31 9858 9868 10.1523/JNEUROSCI.0560-11.2011 Search in Google Scholar

[59] Kawahara M., Ohtsuka I., Yokoyama S., Kato-Negishi M., Sadakane Y.: Membrane incorporation, channel formation, and disruption of calcium homeostasis by Alzheimer’s β-amyloid protein. Int. J. Alzheimers Dis., 2011; 2011: 304583 KawaharaM. OhtsukaI. YokoyamaS. Kato-NegishiM. SadakaneY. Membrane incorporation, channel formation, and disruption of calcium homeostasis by Alzheimer’s β-amyloid protein Int. J. Alzheimers Dis. 2011 2011 304583 Search in Google Scholar

[60] Kenessey A., Nacharaju P., Ko L.W., Yen S.H.: Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration. J. Neurochem., 1997; 69: 2026–2038 KenesseyA. NacharajuP. KoL.W. YenS.H. Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration J. Neurochem. 1997 69 2026 2038 10.1046/j.1471-4159.1997.69052026.x Search in Google Scholar

[61] Khalaf O., Fauvet B., Oueslati A., Dikiy I., Mahul-Mellier A.L., Ruggeri F.S., Mbefo M.K., Vercruysse F., Dietler G., Lee S.J., Eliezer D., Lashuel H.A.: The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity. J. Biol. Chem., 2014; 289: 21856–21876 KhalafO. FauvetB. OueslatiA. DikiyI. Mahul-MellierA.L. RuggeriF.S. MbefoM.K. VercruysseF. DietlerG. LeeS.J. EliezerD. LashuelH.A. The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity J. Biol. Chem. 2014 289 21856 21876 10.1074/jbc.M114.553297 Search in Google Scholar

[62] Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L.: Developmentally regulated expression of specific tau sequences. Neuron, 1989; 2: 1389–1397 KosikK.S. OrecchioL.D. BakalisS. NeveR.L. Developmentally regulated expression of specific tau sequences Neuron 1989 2 1389 1397 10.1016/0896-6273(89)90077-9 Search in Google Scholar

[63] Kühnlein P., Sperfeld A.D., Vanmassenhove B., Van Deerlin V., Lee V.M., Trojanowski J.Q., Kretzschmar H.A., Ludolph A.C., Neumann M.: Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations. Arch. Neurol., 2008; 65: 1185–1189 KühnleinP. SperfeldA.D. VanmassenhoveB. Van DeerlinV. LeeV.M. TrojanowskiJ.Q. KretzschmarH.A. LudolphA.C. NeumannM. Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations Arch. Neurol. 2008 65 1185 1189 10.1001/archneur.65.9.1185274297618779421 Search in Google Scholar

[64] Kumar S., Jangir D.K., Kumar R., Kumari M., Bhavesh N.S., Maiti T.K.: Role of sporadic Parkinson disease associated mutations A18T and A29S in enhanced α-synuclein fibrillation and cytotoxicity. ACS Chem. Neurosci., 2018; 9: 230–240 KumarS. JangirD.K. KumarR. KumariM. BhaveshN.S. MaitiT.K. Role of sporadic Parkinson disease associated mutations A18T and A29S in enhanced α-synuclein fibrillation and cytotoxicity ACS Chem. Neurosci. 2018 9 230 240 10.1021/acschemneuro.6b0043028841377 Search in Google Scholar

[65] Lei P., Ayton S., Finkelstein D.I., Spoerri L., Ciccotosto G.D., Wright D.K., Wong B.X., Adlard P.A., Cherny R.A., Lam L.Q., Roberts B.R., Volitakis I., Egan G.F., McLean C.A., Cappai R. i wsp.: Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export. Nat. Med., 2012; 18: 291–295 LeiP. AytonS. FinkelsteinD.I. SpoerriL. CiccotostoG.D. WrightD.K. WongB.X. AdlardP.A. ChernyR.A. LamL.Q. RobertsB.R. VolitakisI. EganG.F. McLeanC.A. CappaiR. Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export Nat. Med. 2012 18 291 295 10.1038/nm.261322286308 Search in Google Scholar

[66] Liu F., Grundke-Iqbal I., Iqbal K., Gong C.X.: Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur. J. Neurosci., 2005; 22: 1942–1950 LiuF. Grundke-IqbalI. IqbalK. GongC.X. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation Eur. J. Neurosci. 2005 22 1942 1950 10.1111/j.1460-9568.2005.04391.x16262633 Search in Google Scholar

[67] Liu Y., Lv K., Li Z., Yu A.C., Chen J., Teng J.: PACSIN1, a Tau-interacting protein, regulates axonal elongation and branching by facilitating microtubule instability. J. Biol. Chem., 2012; 287: 39911–39924 LiuY. LvK. LiZ. YuA.C. ChenJ. TengJ. PACSIN1, a Tau-interacting protein, regulates axonal elongation and branching by facilitating microtubule instability J. Biol. Chem. 2012 287 39911 39924 10.1074/jbc.M112.403451350107223035120 Search in Google Scholar

[68] Lu J., Duan W., Guo Y., Jiang H., Li Z., Huang J., Hong K., Li C.: Mitochondrial dysfunction in human TDP-43 transfected NSC34 cell lines and the protective effect of dimethoxy curcumin. Brain Res. Bull., 2012; 89: 185–190 LuJ. DuanW. GuoY. JiangH. LiZ. HuangJ. HongK. LiC. Mitochondrial dysfunction in human TDP-43 transfected NSC34 cell lines and the protective effect of dimethoxy curcumin Brain Res. Bull. 2012 89 185 190 10.1016/j.brainresbull.2012.09.00522986236 Search in Google Scholar

[69] Lundblad M., Decressac M., Mattsson B., Björklund A.: Impaired neurotransmission caused by overexpression of α-synuclein in nigral dopamine neurons. Proc. Natl. Acad. Sci. USA, 2012; 109: 3213–3219 LundbladM. DecressacM. MattssonB. BjörklundA. Impaired neurotransmission caused by overexpression of α-synuclein in nigral dopamine neurons Proc. Natl. Acad. Sci. USA 2012 109 3213 3219 10.1073/pnas.1200575109 Search in Google Scholar

[70] Maroteaux L., Campanelli J.T., Scheller R.H.: Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci., 1988; 8: 2804–2815 MaroteauxL. CampanelliJ.T. SchellerR.H. Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal J. Neurosci. 1988 8 2804 2815 10.1523/JNEUROSCI.08-08-02804.1988 Search in Google Scholar

[71] Martin L., Latypova X., Terro F.: Post-translational modifications of tau protein: Implications for Alzheimer’s disease. Neurochem. Int., 2011; 58: 458–471 MartinL. LatypovaX. TerroF. Post-translational modifications of tau protein: Implications for Alzheimer’s disease Neurochem. Int. 2011 58 458 471 10.1016/j.neuint.2010.12.023 Search in Google Scholar

[72] Matsuoka Y., Picciano M., Malester B., LaFrancois J., Zehr C., Daeschner J.M., Olschowka J.A., Fonseca M.I., O’Banion M.K., Tenner A.J., Lemere C.A., Duff K.: Inflammatory responses to amyloidosis in a transgenic mouse model of Alzheimer’s disease. Am. J. Pathol., 2001; 158: 1345–1354 MatsuokaY. PiccianoM. MalesterB. LaFrancoisJ. ZehrC. DaeschnerJ.M. OlschowkaJ.A. FonsecaM.I. O’BanionM.K. TennerA.J. LemereC.A. DuffK. Inflammatory responses to amyloidosis in a transgenic mouse model of Alzheimer’s disease Am. J. Pathol. 2001 158 1345 1354 10.1016/S0002-9440(10)64085-0 Search in Google Scholar

[73] Meade R.M., Fairlie D.P., Mason J.M.: Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles. Mol. Neurodegener., 2019; 14: 29 MeadeR.M. FairlieD.P. MasonJ.M. Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles Mol. Neurodegener. 2019 14 29 10.1186/s13024-019-0329-1664717431331359 Search in Google Scholar

[74] Mena R., Luna-Muñoz J.C.: Stages of pathological tau-protein processing in Alzheimer’s disease: From soluble aggregations to polymerization into insoluble Tau-PHFs. W: Current Hypotheses and Research Milestones in Alzheimer’s Disease, red.: R.B. Maccoini, G. Perry. Springer US, New York 2009, 79–91 MenaR. Luna-MuñozJ.C. Stages of pathological tau-protein processing in Alzheimer’s disease: From soluble aggregations to polymerization into insoluble Tau-PHFs W: Current Hypotheses and Research Milestones in Alzheimer’s Disease red.: MaccoiniR.B. PerryG. Springer US, New York 2009 79 91 10.1007/978-0-387-87995-6_7 Search in Google Scholar

[75] Min S.W., Cho S.H., Zhou Y., Schroeder S., Haroutunian V., Seeley W.W., Huang E.J., Shen Y., Masliah E., Mukherjee C., Meyers D., Cole P.A., Ott M., Gan L.: Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron, 2010; 67: 953–966 MinS.W. ChoS.H. ZhouY. SchroederS. HaroutunianV. SeeleyW.W. HuangE.J. ShenY. MasliahE. MukherjeeC. MeyersD. ColeP.A. OttM. GanL. Acetylation of tau inhibits its degradation and contributes to tauopathy Neuron 2010 67 953 966 10.1016/j.neuron.2010.08.044303510320869593 Search in Google Scholar

[76] Mohite G.M., Navalkar A., Kumar R., Mehra S., Das S., Gadhe L.G., Ghosh D., Alias B., Chandrawanshi V., Ramakrishnan A., Mehra S., Maji S.K.: The familial α-synuclein A53E mutation enhances cell death in response to environmental toxins due to a larger population of oligomers. Biochemistry, 2018; 57: 5014–5028 MohiteG.M. NavalkarA. KumarR. MehraS. DasS. GadheL.G. GhoshD. AliasB. ChandrawanshiV. RamakrishnanA. MehraS. MajiS.K. The familial α-synuclein A53E mutation enhances cell death in response to environmental toxins due to a larger population of oligomers Biochemistry 2018 57 5014 5028 10.1021/acs.biochem.8b0032130025458 Search in Google Scholar

[77] Neumann M., Kwong L.K., Lee E.B., Kremmer E., Flatley A., Xu Y., Forman M.S., Troost D., Kretzschmar H.A., Trojanowski J.Q., Lee V.M.: Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol., 2009; 117: 137–149 NeumannM. KwongL.K. LeeE.B. KremmerE. FlatleyA. XuY. FormanM.S. TroostD. KretzschmarH.A. TrojanowskiJ.Q. LeeV.M. Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies Acta Neuropathol. 2009 117 137 149 10.1007/s00401-008-0477-9269362519125255 Search in Google Scholar

[78] Neumann M., Sampathu D.M., Kwong L.K., Truax A.C., Micsenyi M.C., Chou T.T., Bruce J., Schuck T., Grossman M., Clark C.M., McCluskey L.F., Miller B.L., Masliah E., Mackenzie I.R., Feldman H. i wsp.: Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science, 2006; 314: 130–133 NeumannM. SampathuD.M. KwongL.K. TruaxA.C. MicsenyiM.C. ChouT.T. BruceJ. SchuckT. GrossmanM. ClarkC.M. McCluskeyL.F. MillerB.L. MasliahE. MackenzieI.R. FeldmanH. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis Science 2006 314 130 133 10.1126/science.113410817023659 Search in Google Scholar

[79] Neve R.L., Harris P., Kosik K.S., Kurnit D.M., Donlon T.A.: Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain. Res., 1986; 387: 271–280 NeveR.L. HarrisP. KosikK.S. KurnitD.M. DonlonT.A. Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2 Brain. Res. 1986 387 271 280 10.1016/0169-328X(86)90033-1 Search in Google Scholar

[80] Ou S.H., Wu F., Harrich D., García-Martínez L.F., Gaynor R.B.: Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol., 1995; 69: 3584–3596 OuS.H. WuF. HarrichD. García-MartínezL.F. GaynorR.B. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs J. Virol. 1995 69 3584 3596 10.1128/jvi.69.6.3584-3596.19951890737745706 Search in Google Scholar

[81] Ozer R.S., Halpain S.: Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton. Mol. Biol. Cell, 2000; 11: 3573–3587 OzerR.S. HalpainS. Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton Mol. Biol. Cell 2000 11 3573 3587 10.1091/mbc.11.10.35731501411029056 Search in Google Scholar

[82] Pandey N., Schmidt R.E., Galvin J.E.: The alpha-synuclein mutation E46K promotes aggregation in cultured cells. Exp. Neurol., 2006; 197: 515–520 PandeyN. SchmidtR.E. GalvinJ.E. The alpha-synuclein mutation E46K promotes aggregation in cultured cells Exp. Neurol. 2006 197 515 520 10.1016/j.expneurol.2005.10.01916325180 Search in Google Scholar

[83] Pesiridis G.S., Lee V.M., Trojanowski J.Q.: Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet., 2009; 18: R156–R162 PesiridisG.S. LeeV.M. TrojanowskiJ.Q. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis Hum. Mol. Genet. 2009 18 R156 R162 10.1093/hmg/ddp303 Search in Google Scholar

[84] Pinarbasi E.S., Cağatay T., Fung H.Y.J., Li Y.C., Chook Y.M., Thomas P.J.: Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization. Sci. Rep., 2018; 8: 7083 PinarbasiE.S. CağatayT. FungH.Y.J. LiY.C. ChookY.M. ThomasP.J. Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization Sci. Rep. 2018 8 7083 10.1038/s41598-018-25008-4 Search in Google Scholar

[85] Plotegher N., Kumar D., Tessari I., Brucale M., Munari F., Tosatto L., Belluzzi E., Greggio E., Bisaglia M., Capaldi S., Aioanei D., Mammi S., Monaco H.L., Samo B., Bubacco L.: The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity. Hum. Mol. Genet., 2014; 23: 5615–5629 PlotegherN. KumarD. TessariI. BrucaleM. MunariF. TosattoL. BelluzziE. GreggioE. BisagliaM. CapaldiS. AioaneiD. MammiS. MonacoH.L. SamoB. BubaccoL. The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity Hum. Mol. Genet. 2014 23 5615 5629 10.1093/hmg/ddu275 Search in Google Scholar

[86] Polymenidou M., Lagier-Tourenne C., Hutt K.R., Huelga S.C., Moran J., Liang T.Y., Ling S.C., Sun E., Wancewicz E., Mazur C., Kordasiewicz H., Sedaghat Y., Donohue J.P., Shiue L., Bennett C.F. i wsp.: Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat. Neurosci., 2011; 14: 459–468 PolymenidouM. Lagier-TourenneC. HuttK.R. HuelgaS.C. MoranJ. LiangT.Y. LingS.C. SunE. WancewiczE. MazurC. KordasiewiczH. SedaghatY. DonohueJ.P. ShiueL. BennettC.F. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43 Nat. Neurosci. 2011 14 459 468 10.1038/nn.2779 Search in Google Scholar

[87] Prasad A., Sivalingam V., Bharathi V., Girdhar A., Patel B.K.: The amyloidogenicity of a C-terminal region of TDP-43 implicated in amyotrophic lateral sclerosis can be affected by anions, acetylation and homodimerization. Biochimie, 2018; 150: 76–87 PrasadA. SivalingamV. BharathiV. GirdharA. PatelB.K. The amyloidogenicity of a C-terminal region of TDP-43 implicated in amyotrophic lateral sclerosis can be affected by anions, acetylation and homodimerization Biochimie 2018 150 76 87 10.1016/j.biochi.2018.05.003 Search in Google Scholar

[88] Qureshi H.Y., Paudel H.K.: Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and α-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro. J. Biol. Chem., 2011; 286: 5055–5068 QureshiH.Y. PaudelH.K. Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and α-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro J. Biol. Chem. 2011 286 5055 5068 10.1074/jbc.M110.178905 Search in Google Scholar

[89] Ramaswami M., Taylor J.P., Parker R.: Altered ribostasis: RNA-protein granules in degenerative disorders. Cell, 2013; 154: 727–736 RamaswamiM. TaylorJ.P. ParkerR. Altered ribostasis: RNA-protein granules in degenerative disorders Cell 2013 154 727 736 10.1016/j.cell.2013.07.038 Search in Google Scholar

[90] Rocca W.A.: The burden of Parkinson’s disease: A worldwide perspective. Lancet Neurol., 2018; 17: 928–929 RoccaW.A. The burden of Parkinson’s disease: A worldwide perspective Lancet Neurol. 2018 17 928 929 10.1016/S1474-4422(18)30355-7 Search in Google Scholar

[91] Russo M.A., Tomino C., Vernucci E., Limana F., Sansone L., Frustaci A., Tafani M.: Hypoxia and inflammation as a consequence of β-fibril accumulation: A perspective view for new potential therapeutic targets. Oxid. Med. Cell. Longev., 2019; 2019: 7935310 RussoM.A. TominoC. VernucciE. LimanaF. SansoneL. FrustaciA. TafaniM. Hypoxia and inflammation as a consequence of β-fibril accumulation: A perspective view for new potential therapeutic targets Oxid. Med. Cell. Longev. 2019 2019 7935310 10.1155/2019/7935310661834831346362 Search in Google Scholar

[92] Salvatori I., Ferri A., Scaricamazza S., Giovannelli I., Serrano A., Rossi S., D’Ambrosi N., Cozzolino M., Giulio A.D., Moreno S., Valle C., Carrì M.T.: Differential toxicity of TAR DNA-binding protein 43 iso-forms depends on their submitochondrial localization in neuronal cells. J. Neurochem., 2018; 146: 585–597 SalvatoriI. FerriA. ScaricamazzaS. GiovannelliI. SerranoA. RossiS. D’AmbrosiN. CozzolinoM. GiulioA.D. MorenoS. ValleC. CarrìM.T. Differential toxicity of TAR DNA-binding protein 43 iso-forms depends on their submitochondrial localization in neuronal cells J. Neurochem. 2018 146 585 597 10.1111/jnc.1446529779213 Search in Google Scholar

[93] Saman S., Kim W., Raya M., Visnick Y., Miro S., Saman S., Jackson B., McKee A.C., Alvarez V.E., Lee N.C., Hall G.F.: Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J. Biol. Chem., 2012; 287: 3842–3849 SamanS. KimW. RayaM. VisnickY. MiroS. SamanS. JacksonB. McKeeA.C. AlvarezV.E. LeeN.C. HallG.F. Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease J. Biol. Chem. 2012 287 3842 3849 10.1074/jbc.M111.277061328168222057275 Search in Google Scholar

[94] Siddiqui I.J., Pervaiz N., Abbasi A.A.: The Parkinson Disease gene SNCA: Evolutionary and structural insights with pathological implication. Sci. Rep., 2016; 6: 24475 SiddiquiI.J. PervaizN. AbbasiA.A. The Parkinson Disease gene SNCA: Evolutionary and structural insights with pathological implication Sci. Rep. 2016 6 24475 10.1038/srep24475483224627080380 Search in Google Scholar

[95] Singleton A.B., Farrer M., Johnson J., Singleton A., Hague S., Kachergus J., Hulihan M., Peuralinna T., Dutra A., Nussbaum R., Lincoln S., Crawley A., Hanson M., Maraganore D., Adler C. i wsp.: α-synuclein locus triplication causes Parkinson’s disease. Science, 2003; 302: 841 SingletonA.B. FarrerM. JohnsonJ. SingletonA. HagueS. KachergusJ. HulihanM. PeuralinnaT. DutraA. NussbaumR. LincolnS. CrawleyA. HansonM. MaraganoreD. AdlerC. α-synuclein locus triplication causes Parkinson’s disease Science 2003 302 841 10.1126/science.109027814593171 Search in Google Scholar

[96] Spillantini M.G., Divane A., Goedert M.: Assignment of human α-synuclein (SNCA) and β-synuclein (SNCB) genes to chromosomes 4q21 and 5q35. Genomics, 1995; 27: 379–381 SpillantiniM.G. DivaneA. GoedertM. Assignment of human α-synuclein (SNCA) and β-synuclein (SNCB) genes to chromosomes 4q21 and 5q35 Genomics 1995 27 379 381 10.1006/geno.1995.10637558013 Search in Google Scholar

[97] Sprovieri T., Ungaro C., Perrone B., Naimo G.D., Spataro R., Cavallaro S., La Bella V., Conforti F.L.: A novel S379A TARDBP mutation associated to late-onset sporadic ALS. Neurol. Sci., 2019; 40: 2111–2118 SprovieriT. UngaroC. PerroneB. NaimoG.D. SpataroR. CavallaroS. La BellaV. ConfortiF.L. A novel S379A TARDBP mutation associated to late-onset sporadic ALS Neurol. Sci. 2019 40 2111 2118 10.1007/s10072-019-03943-y31165305 Search in Google Scholar

[98] Stefanoska K., Volkerling A., Bertz J., Poljak A., Ke Y.D., Ittner L.M., Ittner A.: An N-terminal motif unique to primate tau enables differential protein-protein interactions. J. Biol. Chem., 2018; 293: 3710–3719 StefanoskaK. VolkerlingA. BertzJ. PoljakA. KeY.D. IttnerL.M. IttnerA. An N-terminal motif unique to primate tau enables differential protein-protein interactions J. Biol. Chem. 2018 293 3710 3719 10.1074/jbc.RA118.001784584616329382714 Search in Google Scholar

[99] Strang K.H., Golde T.E., Giasson B.I.: MAPT mutations, tauopathy, and mechanisms of neurodegeneration. Lab. Invest., 2019; 99: 912–928 StrangK.H. GoldeT.E. GiassonB.I. MAPT mutations, tauopathy, and mechanisms of neurodegeneration Lab. Invest. 2019 99 912 928 10.1038/s41374-019-0197-x728937230742061 Search in Google Scholar

[100] Sultan A., Nesslany F., Violet M., Bégard S., Loyens A., Talahari S., Mansuroglu Z., Marzin D., Sergeant N., Humez S., Colin M., Bonnefoy E., Buée L., Galas M.C.: Nuclear tau, a key player in neuronal DNA protection. J. Biol. Chem., 2011; 286: 4566–4575 SultanA. NesslanyF. VioletM. BégardS. LoyensA. TalahariS. MansurogluZ. MarzinD. SergeantN. HumezS. ColinM. BonnefoyE. BuéeL. GalasM.C. Nuclear tau, a key player in neuronal DNA protection J. Biol. Chem. 2011 286 4566 4575 10.1074/jbc.M110.199976303939821131359 Search in Google Scholar

[101] Takeda T.: Possible concurrence of TDP-43, tau and other proteins in amyotrophic lateral sclerosis/frontotemporal lobar degeneration. Neuropathology, 2018; 38: 72–81 TakedaT. Possible concurrence of TDP-43, tau and other proteins in amyotrophic lateral sclerosis/frontotemporal lobar degeneration Neuropathology 2018 38 72 81 10.1111/neup.1242828960544 Search in Google Scholar

[102] TARDBP TAR DNA binding protein [Homo sapiens (human)] – Gene – NCBI. https://www.ncbi.nlm.nih.gov/gene/23435 (02.06.2020) TARDBP TAR DNA binding protein [Homo sapiens (human)] – Gene – NCBI https://www.ncbi.nlm.nih.gov/gene/23435 (02.06.2020) Search in Google Scholar

[103] Turner B.J., Bäumer D., Parkinson N.J., Scaber J., Ansorge O., Talbot K.: TDP-43 expression in mouse models of amyotrophic lateral sclerosis and spinal muscular atrophy. BMC Neurosci., 2008; 9: 104 TurnerB.J. BäumerD. ParkinsonN.J. ScaberJ. AnsorgeO. TalbotK. TDP-43 expression in mouse models of amyotrophic lateral sclerosis and spinal muscular atrophy BMC Neurosci. 2008 9 104 10.1186/1471-2202-9-104258398018957104 Search in Google Scholar

[104] van Swieten J., Spillantini M.G.: Hereditary frontotemporal dementia caused by Tau gene mutations. Brain Pathol., 2007; 17: 63–73 van SwietenJ. SpillantiniM.G. Hereditary frontotemporal dementia caused by Tau gene mutations Brain Pathol. 2007 17 63 73 10.1111/j.1750-3639.2007.00052.x809560817493040 Search in Google Scholar

[105] Vicente Miranda H., Cássio R., Correia-Guedes L., Gomes M.A., Chegão A., Miranda E., Soares T., Coelho M., Rosa M.M., Ferreira J.J., Outeiro T.F.: Posttranslational modifications of blood-derived alpha-synuclein as biochemical markers for Parkinson’s disease. Sci. Rep., 2017; 7: 13713 Vicente MirandaH. CássioR. Correia-GuedesL. GomesM.A. ChegãoA. MirandaE. SoaresT. CoelhoM. RosaM.M. FerreiraJ.J. OuteiroT.F. Posttranslational modifications of blood-derived alpha-synuclein as biochemical markers for Parkinson’s disease Sci. Rep. 2017 7 13713 10.1038/s41598-017-14175-5 Search in Google Scholar

[106] von Bergen M., Barghorn S., Biernat J., Mandelkow E.M., Mandelkow E.: Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim. Biophys. Acta, 2005; 1739: 158–166 von BergenM. BarghornS. BiernatJ. MandelkowE.M. MandelkowE. Tau aggregation is driven by a transition from random coil to beta sheet structure Biochim. Biophys. Acta 2005 1739 158 166 10.1016/j.bbadis.2004.09.010 Search in Google Scholar

[107] Wang Y.T., Kuo P.H., Chiang C.H., Liang J.R., Chen Y.R., Wang S., Shen J.C., Yuan H.S.: The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates. J. Biol. Chem., 2013; 288: 9049–9057 WangY.T. KuoP.H. ChiangC.H. LiangJ.R. ChenY.R. WangS. ShenJ.C. YuanH.S. The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates J. Biol. Chem. 2013 288 9049 9057 10.1074/jbc.M112.438564 Search in Google Scholar

[108] Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M., Titani K., Arai T., Kosik K.S., Ihara Y.: In vivo phosphorylation sites in fetal and adult rat tau. J. Biol. Chem., 1993; 268: 25712–25717 WatanabeA. HasegawaM. SuzukiM. TakioK. Morishima-KawashimaM. TitaniK. AraiT. KosikK.S. IharaY. In vivo phosphorylation sites in fetal and adult rat tau J. Biol. Chem. 1993 268 25712 25717 10.1016/S0021-9258(19)74447-0 Search in Google Scholar

[109] Wilhelmsen K.C., Lynch T., Pavlou E., Higgins M., Nygaard T.G.: Localization of disinhibition-dementia-parkinsonism-amyotrophy complex to 17q21–22. Am. J. Hum. Genet., 1994; 55: 1159–1165 WilhelmsenK.C. LynchT. PavlouE. HigginsM. NygaardT.G. Localization of disinhibition-dementia-parkinsonism-amyotrophy complex to 17q21–22 Am. J. Hum. Genet. 1994 55 1159 1165 Search in Google Scholar

[110] Wong Y.C., Krainc D.: α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies. Nat. Med., 2017; 23: 1–13 WongY.C. KraincD. α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies Nat. Med. 2017 23 1 13 10.1038/nm.4269848019728170377 Search in Google Scholar

[111] Yamada K., Holth J.K., Liao F., Stewart F.R., Mahan T.E., Jiang H., Cirrito J.R., Patel T.K., Hochgräfe K., Mandelkow E.M., Holtzman D.M.: Neuronal activity regulates extracellular tau in vivo. J. Exp. Med., 2014; 211: 387–393 YamadaK. HolthJ.K. LiaoF. StewartF.R. MahanT.E. JiangH. CirritoJ.R. PatelT.K. HochgräfeK. MandelkowE.M. HoltzmanD.M. Neuronal activity regulates extracellular tau in vivo J. Exp. Med. 2014 211 387 393 10.1084/jem.20131685394956424534188 Search in Google Scholar

[112] Yang W., Wang X., Duan C., Lu L., Yang H.: Alpha-synuclein over-expression increases phosphoprotein phosphatase 2A levels via formation of calmodulin/Src complex. Neurochem. Int., 2013; 63: 180–194 YangW. WangX. DuanC. LuL. YangH. Alpha-synuclein over-expression increases phosphoprotein phosphatase 2A levels via formation of calmodulin/Src complex Neurochem. Int. 2013 63 180 194 10.1016/j.neuint.2013.06.01023796501 Search in Google Scholar

[113] Yarchoan M., Toledo J.B., Lee E.B., Arvanitakis Z., Kazi H., Han L.Y., Louneva N., Lee V.M., Kim S.F., Trojanowski J.Q., Arnold S.E.: Abnormal serine phosphorylation of insulin receptor substrate 1 is associated with tau pathology in Alzheimer’s disease and tauopathies. Acta Neuropathol., 2014; 128: 679–689 YarchoanM. ToledoJ.B. LeeE.B. ArvanitakisZ. KaziH. HanL.Y. LounevaN. LeeV.M. KimS.F. TrojanowskiJ.Q. ArnoldS.E. Abnormal serine phosphorylation of insulin receptor substrate 1 is associated with tau pathology in Alzheimer’s disease and tauopathies Acta Neuropathol. 2014 128 679 689 10.1007/s00401-014-1328-5430465825107476 Search in Google Scholar

[114] Yuan A., Kumar A., Peterhoff C., Duff K., Nixon R.A.: Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice. J. Neurosci., 2008; 28: 1682–1687 YuanA. KumarA. PeterhoffC. DuffK. NixonR.A. Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice J. Neurosci. 2008 28 1682 1687 10.1523/JNEUROSCI.5242-07.2008281445418272688 Search in Google Scholar

[115] Yuzwa S.A., Macauley M.S., Heinonen J.E., Shan X., Dennis R.J., He Y., Whitworth G.E., Stubbs K.A., McEachern E.J., Davies G.J., Vocadlo D.J.: A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat. Chem. Biol., 2008; 4: 483–490 YuzwaS.A. MacauleyM.S. HeinonenJ.E. ShanX. DennisR.J. HeY. WhitworthG.E. StubbsK.A. McEachernE.J. DaviesG.J. VocadloD.J. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo Nat. Chem. Biol. 2008 4 483 490 10.1038/nchembio.96 Search in Google Scholar

[116] Zarranz J.J., Alegre J., Gómez-Esteban J.C., Lezcano E., Ros R., Ampuero I., Vidal L., Hoenicka J., Rodriguez O., Atarés B., Llorens V., Gomez Tortosa E., del Ser T., Muñoz D.G., de Yebenes J.G.: The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol., 2004; 55: 164–173 ZarranzJ.J. AlegreJ. Gómez-EstebanJ.C. LezcanoE. RosR. AmpueroI. VidalL. HoenickaJ. RodriguezO. AtarésB. LlorensV. Gomez TortosaE. del SerT. MuñozD.G. de YebenesJ.G. The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia Ann. Neurol. 2004 55 164 173 10.1002/ana.10795 Search in Google Scholar

[117] Zempel H., Thies E., Mandelkow E., Mandelkow E.M.: Aβ oligomers cause localized Ca²⁺ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J. Neurosci., 2010; 30: 11938–11950 ZempelH. ThiesE. MandelkowE. MandelkowE.M. Aβ oligomers cause localized Ca²⁺ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines J. Neurosci. 2010 30 11938 11950 10.1523/JNEUROSCI.2357-10.2010 Search in Google Scholar

[118] Zhang Y., Chen K., Sloan S.A., Bennett M.L., Scholze A.R., O’Keeffe S., Phatnani H.P., Guarnieri P., Caneda C., Ruderisch N., Deng S., Liddelow S.A., Zhang C., Daneman R., Maniatis T. i wsp.: An RNA-sequencing transcriptome and splicing database of glia, neurons, and vascular cells of the cerebral cortex. J. Neurosci., 2014; 34: 11929–11947 ZhangY. ChenK. SloanS.A. BennettM.L. ScholzeA.R. O’KeeffeS. PhatnaniH.P. GuarnieriP. CanedaC. RuderischN. DengS. LiddelowS.A. ZhangC. DanemanR. ManiatisT. An RNA-sequencing transcriptome and splicing database of glia, neurons, and vascular cells of the cerebral cortex J. Neurosci. 2014 34 11929 11947 10.1523/JNEUROSCI.1860-14.2014 Search in Google Scholar

[119] Zhang Y.W., Thompson R., Zhang H., Xu H.: APP processing in Alzheimer’s disease. Mol. Brain., 2011; 4: 3 ZhangY.W. ThompsonR. ZhangH. XuH. APP processing in Alzheimer’s disease Mol. Brain. 2011 4 3 10.1186/1756-6606-4-3 Search in Google Scholar

[120] Zheng W.H., Bastianetto S., Mennicken F., Ma W., Kar S.: Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures. Neuroscience, 2002; 115: 201–211 ZhengW.H. BastianettoS. MennickenF. MaW. KarS. Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures Neuroscience 2002 115 201 211 10.1016/S0306-4522(02)00404-9 Search in Google Scholar