Receptor 1 fibroblastnog faktora rasta
(Preusmjereno sa stranice FGFR-1)
| edit |
Receptor 1 fibroblastnog faktora rasta (FGFR1, receptor 1 bazičnog fibroblastnog faktora rasta, fms-srodna tirozinska kinaza-2 / Pfeiffer sindrom, i CD331) receptorska tirozinska kinaza je čiji ligandi su specifični članovi familije fibroblastnih faktora rasta. FGFR1 je asocirana sa Pfeiffer sindromom.[1]
Protein kodiran ovim genom je član familije receptora fibroblastnih faktora rasta (FGFR) među kojima je aminokiselinska sekvenca visoko konzervirana tokom evolucije. Članovi FGFR familije se međusobno razlikuju po nihovom afinitetu za ligande i tkivnoj distribuciji. Reprezentativni protein pune dužine se sastoji od ekstracelularnog regiona, sastavljenog od tri imunoglobulinu slična domena, jednog hidrofobnog jednoprolaznog membranskog segmenta i citoplazmatičnog tirozinskog kinaznog domena. Ekstracelularna porcija proteina interaguje sa fibroblastnim faktorima rasta, čime se pokreće signalna kaslada koja utiče na mitogenezu i diferencijaciju. Ovaj član familije se vezuje za kisele i bazne fibroblastne faktore rasta.
Receptor 1 fibroblastnog faktora rasta formira interakcije sa GRB14,[2] SHB,[3] FRS2,[4][5][6][7] Klotho,[8] i FGF1.[9][10]
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Urakawa I, Jamazaki Y, Shimada T, Iijima K, Hasegawa H, Okawa K, Fujita T, Fukumoto S, Yameshita T (October 2006). „Klotho converts canonical FGF receptor into a specific receptor for FGF23”. Nature. 444: 770–4. DOI:10.1038/nature05315. PMID 7086194.
- ↑ 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.
- Weiss J, Sos ML, Seidel D i dr.. (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.
- GeneReviews/NIH/NCBI/UW entry on FGFR-Related Craniosynostosis Syndromes
- GeneReviews/NCBI/NIH/UW entry on Kallmann syndrome
- MeSH FGFR1+protein,+human
- Fibroblast growth factor receptor 1 Arhivirano 2011-10-07 na Wayback Machine-u on the Atlas of Genetics and Cytogenetics in Oncology and Haematology
- FGFR1 human gene location in the UCSC Genome Browser.
- FGFR1 human gene details in the UCSC Genome Browser.
PDB Galerija | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| ||||||||||||||||||||
