Autocatalytic phosphorylation of FGFR3 cysteine mutants

Stable Identifier
R-HSA-2012082
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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Autocatalytic phosphorylation of FGFR3 cysteine mutants
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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
12009017 Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization

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

J Bone Miner Res 2002
9438390 Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I

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

Cell Growth Differ 1998
Participants
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Output
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as an event of
Catalyst Activity

protein tyrosine kinase activity of FGFR3 cysteine mutant dimers [plasma membrane]

Physical Entity
FGFR3 cysteine mutant dimers [plasma membrane] (Homo sapiens)
Activity
protein tyrosine kinase activity (GO:0004713)
Functional status

Gain of function of FGFR3 cysteine mutant dimers [plasma membrane]

Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
bone development disease DOID:0080006
Authored
Rothfels, K  (2012-02-10)
Reviewed
Ezzat, S  (2012-05-15)
Created
Rothfels, K  (2011-11-22)
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