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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1992-12-18
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pubmed:databankReference |
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pubmed:abstractText |
Fibroblast growth factor (FGF) receptor (FGFR) gene family consists of at least four receptor tyrosine kinases that transduce signals important in a variety of developmental and physiological processes related to cell growth and differentiation. Here we have characterized the binding of different FGFs to FGFR-4. Our results establish an FGF binding profile for FGFR-4 with aFGF having the highest affinity, followed by K-FGF/hst-1 and bFGF. In addition, FGF-6 was found to bind to FGFR-4 in ligand competition experiments. Interestingly, the FGFR-4 gene was found to encode only the prototype receptor in a region where both FGFR-1 and FGFR-2 show alternative splicing leading to differences in their ligand binding specificities and to secreted forms of these receptors. Ligands binding to FGFR-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides, which differed from those phosphorylated in FGFR-1-expressing cells. Specifically, the FGFR-1-expressing cells showed a considerably more extensive tyrosine phosphorylation of PLC-gamma than the FGFR-4-expressing cells. Structural and functional specificity within the FGFR family exemplified by FGFR-4 may help to explain how FGFs perform their diverse functions.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1309595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1309608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1316275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1325208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1326315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1373495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-14450081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1652059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1655404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1656221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1667382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1689490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1697263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1709094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1722683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1723680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1846048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1846320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1846977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1847508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1847668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1849109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-1970514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2122465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2161540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2167437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2167438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2172978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2236054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2425435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2432664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2472218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2475908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2544996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2549857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2649847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2957062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-2959959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-3032990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-3211147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-3459165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-3523756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1385111-3574458
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/FGF4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 4,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibroblast Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:geneSymbol |
FGFR
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4273-80
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1385111-Alternative Splicing,
pubmed-meshheading:1385111-Amino Acid Sequence,
pubmed-meshheading:1385111-Binding, Competitive,
pubmed-meshheading:1385111-Cells, Cultured,
pubmed-meshheading:1385111-Cloning, Molecular,
pubmed-meshheading:1385111-Cross-Linking Reagents,
pubmed-meshheading:1385111-Exons,
pubmed-meshheading:1385111-Fibroblast Growth Factor 1,
pubmed-meshheading:1385111-Fibroblast Growth Factor 2,
pubmed-meshheading:1385111-Fibroblast Growth Factor 4,
pubmed-meshheading:1385111-Fibroblast Growth Factors,
pubmed-meshheading:1385111-Growth Substances,
pubmed-meshheading:1385111-Humans,
pubmed-meshheading:1385111-Molecular Sequence Data,
pubmed-meshheading:1385111-Phosphorylation,
pubmed-meshheading:1385111-Precipitin Tests,
pubmed-meshheading:1385111-Protein-Tyrosine Kinases,
pubmed-meshheading:1385111-Proto-Oncogene Proteins,
pubmed-meshheading:1385111-Receptors, Fibroblast Growth Factor,
pubmed-meshheading:1385111-Sequence Homology, Amino Acid,
pubmed-meshheading:1385111-Signal Transduction,
pubmed-meshheading:1385111-Tyrosine
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pubmed:year |
1992
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pubmed:articleTitle |
Fibroblast growth factor receptor-4 shows novel features in genomic structure, ligand binding and signal transduction.
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pubmed:affiliation |
Department of Pathology, University of Helsinki, Finland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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