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The canonical FGF-FGFR signaling system at the molecular level

Patrycja Szybowska

Patrycja Szybowska

  • Department of Tumor Biology Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University HospitalMontebello, Norway
  • Center for Cancer Cell Reprogramming, Institute of Clinical Medicine, Faculty of Medicine, University of OsloMontebello, Norway
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Szybowska, Patrycja
, 
Ellen Margrethe Haugsten

Ellen Margrethe Haugsten

  • Department of Tumor Biology Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University HospitalMontebello, Norway
  • Center for Cancer Cell Reprogramming, Institute of Clinical Medicine, Faculty of Medicine, University of OsloMontebello, Norway
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Haugsten, Ellen Margrethe
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Antoni Wiedlocha

Antoni Wiedlocha

  • Department of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University HospitalMontebello, Norway
  • Center for Cancer Cell Reprogramming, Institute of Clinical Medicine, Faculty of Medicine, University of OsloMontebello, Norway
  • Military Institute of Hygiene and EpidemiologyWarsaw, Poland
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Wiedlocha, Antoni
  
17. Jan. 2022
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Artikel-Kategorie: Review
Online veröffentlicht: 17. Jan. 2022
Seitenbereich: 711 - 719
Eingereicht: 16. Okt. 2020
Akzeptiert: 24. Feb. 2021
DOI: https://doi.org/10.2478/ahem-2021-0024
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© 2021 Patrycja Szybowska et al., published by Sciendo
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Figure 1.

The FGF family. The mammalian FGFs can be divided into three subgroups based on their way of action. The intracrine FGFs are not secreted and remain inside the signaling cell. The paracrine and endocrine FGFs are secreted and bind to receiver cells but the endocrine FGFs mainly play roles in an endocrine manner via the blood circulation system.
The FGF family. The mammalian FGFs can be divided into three subgroups based on their way of action. The intracrine FGFs are not secreted and remain inside the signaling cell. The paracrine and endocrine FGFs are secreted and bind to receiver cells but the endocrine FGFs mainly play roles in an endocrine manner via the blood circulation system.

Figure 2.

A schematic presentation of the structure and the activation of FGFRs. (A) FGFRs consist of two or three extracellular immunoglobulin (Ig)-like domains (IgI-IgIII), a transmembrane domain and an intracellular split tyrosine kinase domain (TKI and TKII). An acid box is located between IgI and IgII. The IgII contains also a heparin binding domain. IgIII in FGFR1-3 is alternatively spliced to IgIIIb or IgIIIc variants. (B) Activation of FGFRs. FGF-FGFR interaction in the presence of heparan sulfate triggers receptor dimerization and activation of the tyrosine kinase domain of the receptors.
A schematic presentation of the structure and the activation of FGFRs. (A) FGFRs consist of two or three extracellular immunoglobulin (Ig)-like domains (IgI-IgIII), a transmembrane domain and an intracellular split tyrosine kinase domain (TKI and TKII). An acid box is located between IgI and IgII. The IgII contains also a heparin binding domain. IgIII in FGFR1-3 is alternatively spliced to IgIIIb or IgIIIc variants. (B) Activation of FGFRs. FGF-FGFR interaction in the presence of heparan sulfate triggers receptor dimerization and activation of the tyrosine kinase domain of the receptors.
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