Autocatalytic phosphorylation of FGFR3 cysteine mutants

Stable Identifier
R-HSA-2012082
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Although each of FGFR3 R248C, S249C, G370C, S371C and Y373C have been shown to undergo ligand-independent dimerization and receptor autophosphorylation, there is conflicting evidence about which mutants also show increased phosphorylation upon ligand stimulation. Mutants showed elevated levels of ligand-independent MAPK pathway activation and supported expression of an in vivo reporter gene (d'Avis, 1998; Adar, 2009).

Literature References
PubMed ID Title Journal Year
9438390 Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I

d'Avis, PY, Robertson, SC, Meyer, AN, Bardwell, WM, Webster, MK, Donoghue, DJ

Cell Growth Differ 1998
12009017 Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization

Adar, R, Monsonego-Ornan, E, David, P, Yayon, A

J Bone Miner Res 2002
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of FGFR3 cysteine mutant dimers [plasma membrane]
Physical Entity
Activity
Disease
Name Identifier Synonyms
bone development disease 0080006
cancer 162 malignant tumor, malignant neoplasm, primary cancer
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