Fibroblast growth factor receptor 1 (FGFR1), also known as basic fibroblast growth factor receptor 1, fms-related tyrosine kinase-2 / Pfeiffer syndrome, and CD331, is a receptor tyrosine kinase whose ligands are specific members of the fibroblast growth factor family. FGFR1 has been shown to be associated with Pfeiffer syndrome.[1]
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Function [link]
The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) 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 consists 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, ultimately influencing mitogenesis and differentiation. This particular family member binds both acidic and basic fibroblast growth factors and is involved in limb induction.
Clinical significance [link]
Mutations in this gene have been associated with Pfeiffer syndrome, Jackson-Weiss syndrome, Antley-Bixler syndrome, osteoglophonic dysplasia, squamous cell lung cancer (14) and autosomal dominant Kallmann syndrome 2. A few DNA sequence variants, including one nonsense mutation, have also been reported in isolated or non-syndromic cleft lip and palate.[2] Clefts are a relatively common feature of Kallman syndrome as well.[3][4] Somatic chromosomal aberrations involving this gene are associated with stem cell myeloproliferative disorder and stem cell leukemia lymphoma syndrome. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.[5]
Interactions [link]
Fibroblast growth factor receptor 1 has been shown to interact with GRB14,[6] SHB,[7] FRS2[8][9][10][11] and FGF1.[12][13]
See also [link]
References [link]
- ^ Itoh N, Terachi T, Ohta M, Seo MK (June 1990). "The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA". Biochem. Biophys. Res. Commun. 169 (2): 680–5. DOI:10.1016/0006-291X(90)90384-Y. PMID 2162671.
- ^ Riley BM, Mansilla MA, Ma J, Daack-Hirsch S, Maher BS, Raffensperger LM, Russo ET, Vieira AR, Dodé C, Mohammadi M, Marazita ML, Murray JC (March 2007). "Impaired FGF signaling contributes to cleft lip and palate". Proc. Natl. Acad. Sci. U.S.A. 104 (11): 4512–7. DOI:10.1073/pnas.0607956104. PMC 1810508. PMID 17360555. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1810508.
- ^ Kim HG, Herrick SR, Lemyre E, Kishikawa S, Salisz JA, Seminara S, MacDonald ME, Bruns GA, Morton CC, Quade BJ, Gusella JF (August 2005). "Hypogonadotropic hypogonadism and cleft lip and palate caused by a balanced translocation producing haploinsufficiency for FGFR1". J. Med. Genet. 42 (8): 666–72. DOI:10.1136/jmg.2004.026989. PMC 1736121. PMID 16061567. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1736121.
- ^ Dodé C, Fouveaut C, Mortier G, Janssens S, Bertherat J, Mahoudeau J, Kottler ML, Chabrolle C, Gancel A, François I, Devriendt K, Wolczynski S, Pugeat M, Pineiro-Garcia A, Murat A, Bouchard P, Young J, Delpech M, Hardelin JP (January 2007). "Novel FGFR1 sequence variants in Kallmann syndrome, and genetic evidence that the FGFR1c isoform is required in olfactory bulb and palate morphogenesis". Hum. Mutat. 28 (1): 97–8. DOI:10.1002/humu.9470. PMID 17154279.
- ^ "Entrez Gene: FGFR1 fibroblast growth factor receptor 1 (fms-related tyrosine kinase 2, Pfeiffer syndrome)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2260.
- ^ Reilly JF, Mickey G, Maher PA (March 2000). "Association of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partner". J. Biol. Chem. 275 (11): 7771–8. DOI:10.1074/jbc.275.11.7771. PMID 10713090.
- ^ Karlsson T, Songyang Z, Landgren E, Lavergne C, Di Fiore PP, Anafi M, Pawson T, Cantley LC, Claesson-Welsh L, Welsh M (April 1995). "Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins". Oncogene 10 (8): 1475–83. PMID 7537362.
- ^ Yan KS, Kuti M, Yan S, Mujtaba S, Farooq A, Goldfarb MP, Zhou MM (May 2002). "FRS2 PTB domain conformation regulates interactions with divergent neurotrophic receptors". J. Biol. Chem. 277 (19): 17088–94. DOI:10.1074/jbc.M107963200. PMID 11877385.
- ^ Ong SH, Guy GR, Hadari YR, Laks S, Gotoh N, Schlessinger J, Lax I (February 2000). "FRS2 Proteins Recruit Intracellular Signaling Pathways by Binding to Diverse Targets on Fibroblast Growth Factor and Nerve Growth Factor Receptors". Mol. Cell. Biol. 20 (3): 979–89. DOI:10.1128/MCB.20.3.979-989.2000. PMC 85215. PMID 10629055. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85215.
- ^ Xu H, Lee KW, Goldfarb M (July 1998). "Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins". J. Biol. Chem. 273 (29): 17987–90. DOI:10.1074/jbc.273.29.17987. PMID 9660748.
- ^ Dhalluin C, Yan KS, Plotnikova O, Lee KW, Zeng L, Kuti M, Mujtaba S, Goldfarb MP, Zhou MM (October 2000). "Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors". Mol. Cell 6 (4): 921–9. DOI:10.1016/S1097-2765(05)00087-0. PMID 11090629.
- ^ Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M (September 2000). "Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization". Mol. Cell 6 (3): 743–50. DOI:10.1016/S1097-2765(00)00073-3. PMID 11030354.
- ^ Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM (January 1996). "Expression and biological activity of mouse fibroblast growth factor-9". J. Biol. Chem. 271 (3): 1726–31. DOI:10.1074/jbc.271.3.1726. PMID 8576175.
Further reading [link]
- Weiss J, Sos ML, Seidel D et al. (December 2010). "Frequent and focal FGFR1 amplification associates with therapeutically tractable FGFR1 dependency in squamous cell lung cancer". Sci Transl Med 2 (62): 62ra93. DOI:10.1126/scitranslmed.3001451. PMID 21160078.
- Johnson DE, Williams LT (1993). "Structural and functional diversity in the FGF receptor multigene family". Adv. Cancer Res.. Advances in Cancer Research 60: 1–41. DOI:10.1016/S0065-230X(08)60821-0. ISBN 978-0-12-006660-5. PMID 8417497.
- Macdonald D, Reiter A, Cross NC (2002). "The 8p11 myeloproliferative syndrome: a distinct clinical entity caused by constitutive activation of FGFR1". Acta Haematol. 107 (2): 101–7. DOI:10.1159/000046639. PMID 11919391.
- Groth C, Lardelli M (2003). "The structure and function of vertebrate fibroblast growth factor receptor 1". Int. J. Dev. Biol. 46 (4): 393–400. PMID 12141425.
- Wilkie AO (2005). "Bad bones, absent smell, selfish testes: the pleiotropic consequences of human FGF receptor mutations". Cytokine Growth Factor Rev. 16 (2): 187–203. DOI:10.1016/j.cytogfr.2005.03.001. PMID 15863034.
External links [link]
- GeneReviews/NIH/NCBI/UW entry on FGFR-Related Craniosynostosis Syndromes
- GeneReviews/NCBI/NIH/UW entry on Kallmann syndrome
- FGFR1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- Fibroblast growth factor receptor 1 on the Atlas of Genetics and Oncology
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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Fibroblast growth factor receptor 4
Fibroblast growth factor receptor 4 is a protein that in humans is encoded by the FGFR4 gene. FGFR4 has also been designated as CD334 (cluster of differentiation 334).
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, ultimately influencing mitogenesis and differentiation. The genomic organization of this gene, compared to members 1-3, encompasses 18 exons rather than 19 or 20. Although alternative splicing has been observed, there is no evidence that the C-terminal half of the IgIII domain of this protein varies between three alternate forms, as indicated for members 1-3. This particular family member preferentially binds acidic fibroblast growth factor and, although its specific function is unknown, it is overexpressed in gynecological tumor samples, suggesting a role in breast and ovarian tumorigenesis.
Fibroblast growth factor receptor 2
Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 (cluster of differentiation 332) is a protein that in humans is encoded by the FGFR2 gene residing on chromosome 10. FGFR2 is a receptor for fibroblast growth factor.
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 consists of an extracellular region, composed of three immunoglobulin 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, ultimately influencing mitogenesis and differentiation. This particular family member is a high-affinity receptor for acidic, basic and/or keratinocyte growth factor, depending on the isoform.
