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Identification of a cysteine-rich receptor for fibroblast growth factors
Identification of a cysteine-rich receptor for fibroblast growth factors.
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The fibroblast growth factor (FGF) family consists of seven members whose activities are thought to be mediated by multiple receptors. Here we describe the cDNA cloning, expression, and characterization of a cysteine-rich FGF receptor (CFR) that is distinct from previously identified FGF receptors. The deduced amino acid sequence for CFR suggests that it is an integral membrane protein containing a large extracellular domain comprising 16 cysteine-rich repeated units and an intracellular domain of 13 amino acids. No reported sequences exhibit significant homologies to either the repeated extracellular motif or to the entire CFR amino acid sequence. Several CFR transcripts are present in embryonic chick tissue, suggesting that CFR undergoes alternate mRNA splicing or that related genes are present. Chinese hamster ovary cells transfected with the CFR cDNA express a 150-kDa polypeptide that binds FGF-1, FGF-2, and FGF-4 but does not bind several non-FGF family members. The high degree of evolutionary conservation among vertebrate CFRs and its ability to bind three different FGFs with high affinity suggest that this unique receptor plays an important role in FGF biology.
Burrus LW, Zuber ME, Lueddecke BA, Olwin BB
Molecular and cellular biology
1992-12-01 00:00
12
12
5600-9
Amino Acid Sequence,Animals,Base Sequence,CHO Cells,Chick Embryo,Cloning, Molecular,Cricetinae,Cysteine,DNA,Humans,Molecular Sequence Data,Protein Biosynthesis,Protein Sorting Signals,Receptors, Fibroblast Growth Factor,Sequence Homology, Amino Acid,Transcription, Genetic,Transfection,Protein Sorting Signals,Receptors, Fibroblast Growth Factor,Cysteine,DNA
Department of Biochemistry, University of Wisconsin, Madison 53706
Mol. Cell. Biol.
NIAMS AR-39467, NIGMS GM07215
0270-7306
874
True
1448090
