View source for Fibroblast growth factor receptor 4

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Fibroblast growth factor receptor 4''' ('''FGFR-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 [[hydrophone|hydrophobic]] membrane-spanning segment and a [[cytoplasm]]ic [[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 [[exon]]s rather than 19 or 20. Although [[alternative splicing]] has been observed, there is no evidence that the [[C-terminus|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.<ref>{{cite web | title = Entrez Gene: FGFR4 fibroblast growth factor receptor 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2264}}</ref> In a meta-analisis study, the functional polymorphism Gly388Arg (rs351855) of FGFR4 was observed to be significantly associated with nodal involvement and overall survival in patients with different types of cancer.<ref>{{cite journal|last=Frullanti|first=E|title=Meta and pooled analyses of FGFR4 Gly388Arg polymorphism as a cancer prognostic factor.|journal=Eur J Cancer Prev|date=2011|volume=20|issue=4|pages=340–347|pmid=21412156 |doi=10.1097/CEJ.0b013e3283457274|s2cid=29668012}}</ref>
==Interactions==
Fibroblast growth factor receptor 4 has been shown to [[Protein-protein interaction|interact]] with [[FGF1]].<ref name=pmid10736564>{{cite journal |last=Loo |first=B B |author2=Darwish K K |author3=Vainikka S S |author4=Saarikettu J J |author5=Vihko P P |author6=Hermonen J J |author7=Goldman A A |author8=Alitalo K K |author9=Jalkanen M M   |date=May 2000 |title=Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4 |journal=Int. J. Biochem. Cell Biol. |volume=32 |issue=5 |pages=489–97 |location = ENGLAND| issn = 1357-2725| pmid = 10736564 |doi=10.1016/S1357-2725(99)00145-4 }}</ref><ref name=pmid10336501>{{cite journal |last=Kan |first=M |author2=Wu X |author3=Wang F |author4=McKeehan W L  |date=May 1999 |title=Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase |journal=J. Biol. Chem. |volume=274 |issue=22 |pages=15947–52 |location = UNITED STATES| issn = 0021-9258| pmid = 10336501 |doi=10.1074/jbc.274.22.15947 |doi-access=free }}</ref>
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
*{{cite journal  |vauthors=Doherty P, Smith P, Walsh FS |title=Shared cell adhesion molecule (CAM) homology domains point to CAMs signalling via FGF receptors. |journal=Perspectives on Developmental Neurobiology |volume=4 |issue= 2–3 |pages= 157–68 |year= 1997 |pmid= 9168198 }}
*{{cite journal  |vauthors=Warrington JA, Bailey SK, Armstrong E |title=A radiation hybrid map of 18 growth factor, growth factor receptor, hormone receptor, or neurotransmitter receptor genes on the distal region of the long arm of chromosome 5 |journal=Genomics |volume=13 |issue= 3 |pages= 803–8 |year= 1992 |pmid= 1322355 |doi=10.1016/0888-7543(92)90156-M  |display-authors=etal}}
*{{cite journal  |vauthors=Armstrong E, Partanen J, Cannizzaro L |title=Localization of the fibroblast growth factor receptor-4 gene to chromosome region 5q33-qter |journal=Genes Chromosomes Cancer |volume=4 |issue= 1 |pages= 94–8 |year= 1992 |pmid= 1377018 |doi=10.1002/gcc.2870040116  |s2cid=6377972 |display-authors=etal}}
*{{cite journal  |vauthors=Vainikka S, Partanen J, Bellosta P |title=Fibroblast growth factor receptor-4 shows novel features in genomic structure, ligand binding and signal transduction |journal=EMBO J. |volume=11 |issue= 12 |pages= 4273–80 |year= 1992 |pmid= 1385111 |doi=  10.1002/j.1460-2075.1992.tb05526.x| pmc=557000  |display-authors=etal}}
*{{cite journal  |vauthors=Partanen J, Mäkelä TP, Eerola E |title=FGFR-4, a novel acidic fibroblast growth factor receptor with a distinct expression pattern |journal=EMBO J. |volume=10 |issue= 6 |pages= 1347–54 |year= 1991 |pmid= 1709094 |doi=  10.1002/j.1460-2075.1991.tb07654.x| pmc=452793  |display-authors=etal}}
*{{cite journal  |vauthors=Holtrich U, Bräuninger A, Strebhardt K, Rübsamen-Waigmann H |title=Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10411–5 |year= 1992 |pmid= 1720539 |doi=10.1073/pnas.88.23.10411  | pmc=52938  |bibcode=1991PNAS...8810411H |doi-access=free }}
*{{cite journal  |vauthors=Partanen J, Mäkelä TP, Alitalo R |title=Putative tyrosine kinases expressed in K-562 human leukemia cells |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 8913–7 |year= 1991 |pmid= 2247464 |doi=10.1073/pnas.87.22.8913  | pmc=55070  |display-authors=etal|bibcode=1990PNAS...87.8913P|doi-access=free }}
*{{cite journal  |vauthors=Vainikka S, Joukov V, Wennström S |title=Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1 |journal=J. Biol. Chem. |volume=269 |issue= 28 |pages= 18320–6 |year= 1994 |doi=10.1016/S0021-9258(17)32309-8 |pmid= 7518429 |display-authors=etal|doi-access=free }}
*{{cite journal  |vauthors=Wen Z, Zhong Z, Darnell JE |title=Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation |journal=Cell |volume=82 |issue= 2 |pages= 241–50 |year= 1995 |pmid= 7543024 |doi=10.1016/0092-8674(95)90311-9  |s2cid=6717533 |doi-access=free }}
*{{cite journal  |vauthors=Quelle FW, Thierfelder W, Witthuhn BA |title=Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor |journal=J. Biol. Chem. |volume=270 |issue= 35 |pages= 20775–80 |year= 1995 |pmid= 7657660 |doi=10.1074/jbc.270.35.20775  |display-authors=etal|doi-access=free }}
*{{cite journal  |vauthors=Ron D, Reich R, Chedid M |title=Fibroblast growth factor receptor 4 is a high affinity receptor for both acidic and basic fibroblast growth factor but not for keratinocyte growth factor |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 5388–94 |year= 1993 |doi=10.1016/S0021-9258(18)53334-2 |pmid= 7680645 |display-authors=etal|doi-access=free }}
*{{cite journal  |vauthors=Shuai K, Stark GR, Kerr IM, Darnell JE |title=A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma |journal=Science |volume=261 |issue= 5129 |pages= 1744–6 |year= 1993 |pmid= 7690989 |doi=10.1126/science.7690989  |bibcode=1993Sci...261.1744S }}
*{{cite journal  |vauthors=Jaakkola S, Salmikangas P, Nylund S |title=Amplification of fgfr4 gene in human breast and gynecological cancers |journal=Int. J. Cancer |volume=54 |issue= 3 |pages= 378–82 |year= 1993 |pmid= 8099571 |doi=10.1002/ijc.2910540305  |s2cid=19513080 |display-authors=etal}}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Reich-Slotky R, Shaoul E, Berman B |title=Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificities |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29813–8 |year= 1996 |pmid= 8530375 |doi=10.1074/jbc.270.50.29813  |display-authors=etal|doi-access=free }}
*{{cite journal  |vauthors=Vainikka S, Joukov V, Klint P, Alitalo K |title=Association of a 85-kDa serine kinase with activated fibroblast growth factor receptor-4 |journal=J. Biol. Chem. |volume=271 |issue= 3 |pages= 1270–3 |year= 1996 |pmid= 8576110 |doi=10.1074/jbc.271.3.1270  |doi-access=free }}
*{{cite journal  |vauthors=Kaptein A, Paillard V, Saunders M |title=Dominant negative stat3 mutant inhibits interleukin-6-induced Jak-STAT signal transduction |journal=J. Biol. Chem. |volume=271 |issue= 11 |pages= 5961–4 |year= 1996 |pmid= 8626374 |doi=10.1074/jbc.271.11.5961  |doi-access=free }}
*{{cite journal  |vauthors=Ornitz DM, Xu J, Colvin JS |title=Receptor specificity of the fibroblast growth factor family |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15292–7 |year= 1996 |pmid= 8663044 |doi=10.1074/jbc.271.25.15292  |display-authors=etal|doi-access=free }}
*{{cite journal  |vauthors=Agnès F, Toux MM, André C, Galibert F |title=Genomic organization of the extracellular coding region of the human FGFR4 and FLT4 genes: evolution of the genes encoding receptor tyrosine kinases with immunoglobulin-like domains |journal=J. Mol. Evol. |volume=45 |issue= 1 |pages= 43–9 |year= 1997 |pmid= 9211733 |doi=10.1007/PL00006199  |bibcode=1997JMolE..45...43A |s2cid=34208733 }}
{{refend}}
==External links==
* {{MeshName|FGFR4+protein,+human}}
{{NLM content}}
{{Clusters of differentiation}}
{{Tyrosine kinases}}
{{Enzymes}}
{{Growth factor receptor modulators}}
{{Portal bar|Biology|border=no}}
[[Category:Clusters of differentiation]]
[[Category:Tyrosine kinase receptors]]