Fibroblast growth factor receptor 3 is a protein that in humans is encoded by the FGFR3 gene. FGFR3 has also been designated as CD333 (cluster of differentiation 333).
Structure and function
The protein encoded by this gene is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals which ultimately influencing cell mitogenesis and differentiation.
This particular family member binds both acidic and basic fibroblast growth factor and plays a role in bone development and maintenance. Mutations in this gene lead to craniosynostosis and multiple types of skeletal dysplasia (Osteochondrodysplasia). Alternative splicing occurs and additional variants have been described, including those utilizing alternate exon 8 rather than 9, but their full-length nature has not been determined.
Defects in the FGFR3 gene has been associated with several conditions, including:
Fibroblast growth factor receptor 3 has been shown to interact with FGF1 and FGF9.
- ^ Keegan K, Johnson DE, Williams LT, Hayman MJ (Mar 1991). "Isolation of an additional member of the fibroblast growth factor receptor family, FGFR-3". Proc Natl Acad Sci U S A 88 (4): 1095–9. PMC 50963. PMID 1847508. doi:10.1073/pnas.88.4.1095.
- ^ "Entrez Gene: FGFR3 fibroblast growth factor receptor 3 (achondroplasia, thanatophoric dwarfism)".
- ^ Hafner C, Hartmann A, Vogt T (2007). "FGFR3 mutations in epidermal nevi and seborrheic keratoses: lessons from urothelium and skin". J. Invest. Dermatol. 127 (7): 1572–3. PMID 17568799. doi:10.1038/sj.jid.5700772.
- ^ Lamy A, Gobet F, Laurent M et al. (2006). "Molecular profiling of bladder tumors based on the detection of FGFR3 and TP53 mutations". J. Urol. 176 (6 Pt 1): 2686–9. PMID 17085196. doi:10.1016/j.juro.2006.07.132.
- ^ Mulliken, JB (Nov 1999). "Molecular diagnosis of bilateral coronal synostosis". Plast Reconstr Surg. 104 (6): 1603–1615. PMID 10541159. Retrieved 30 October 2014.
- ^ a b Santos-Ocampo, S; Colvin J S; Chellaiah A; Ornitz D M (Jan 1996). "Expression and biological activity of mouse fibroblast growth factor-9". J. Biol. Chem. (UNITED STATES) 271 (3): 1726–31. ISSN 0021-9258. PMID 8576175. doi:10.1074/jbc.271.3.1726.
- ^ a b Chellaiah, A; Yuan W; Chellaiah M; Ornitz D M (Dec 1999). "Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity". J. Biol. Chem. (UNITED STATES) 274 (49): 34785–94. ISSN 0021-9258. PMID 10574949. doi:10.1074/jbc.274.49.34785.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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