Fibroblast Growth Factor Receptor‐4 Splice Variants Cause Deletion of a Critical Tyrosine

WRA Van Heumen, C Claxton, JO Pickles - IUBMB life, 1999 - Wiley Online Library
WRA Van Heumen, C Claxton, JO Pickles
IUBMB life, 1999Wiley Online Library
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 …
Abstract
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.
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