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Fibroblast Growth Factor Receptor‐4 Splice Variants Cause Deletion of a Critical Tyrosine
Author(s) -
Van Heumen Walter R. A.,
Claxton Christina,
Pickles James O.
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/713803466
Subject(s) - fibroblast growth factor receptor 4 , fibroblast growth factor receptor , intron , gene isoform , biology , fibroblast growth factor receptor 3 , fibroblast growth factor receptor 2 , fgf1 , rna splicing , splice , receptor tyrosine kinase , fibroblast growth factor , alternative splicing , microbiology and biotechnology , genetics , signal transduction , receptor , gene , rna
We have identified two novel isoforms of fibroblast growth factor receptor‐4 (FGFR4). They result from alternative splicing of intron 17. Two transcripts, both slightly larger than the one coding for the known mouse FGFR4, are generated. The shortest (FGFR4‐17a) includes the 31‐most 3‐nucleotides of intron 17; the longest (FGFR4‐17b) includes all 114 nucleotides of intron 17. Translation of the FGFR4‐17a and FGFR4‐17b splice variants predicts that both novel putative FGFR4 isoforms have a truncated C‐terminal intracellular tail. The first amino acid residue affected by the insertions in both novel isoforms is Tyr‐760, a residue that may play a crucial role in intracellular signaling through stimulation of the phosphatidylinositol‐biphosphate pathway.