The expression of two isoforms of the human fibroblast growth factor receptor (flg) is directed by alternative splicing

1991 ◽  
Vol 174 (2) ◽  
pp. 946-951 ◽  
Author(s):  
Hiroko Fujita ◽  
Mitsuhiro Ohta ◽  
Toshisuke Kawasaki ◽  
Nobuyuki Itoh
Keyword(s):  
Alternative Splicing ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Human Fibroblast ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth

Control of BEK and K-SAM splice sites in alternative splicing of the fibroblast growth factor receptor 2 pre-mRNA

1993 ◽  
Vol 13 (9) ◽  
pp. 5461-5468
Author(s):  
E Gilbert ◽  
F Del Gatto ◽  
P Champion-Arnaud ◽  
M C Gesnel ◽  
R Breathnach
Keyword(s):  
Alternative Splicing ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fibroblast Growth ◽  
Splice Sites ◽  
Polypyrimidine Tract ◽  
Profound Influence ◽  
In Cells

The fibroblast growth factor receptor 2 gene pre-mRNA can be spliced by using either the K-SAM exon or the BEK exon. The exon chosen has a profound influence on the ligand-binding specificity of the receptor obtained. Cells make a choice between the two alternative exons by controlling use of both exons. Using fibroblast growth factor receptor 2 minigenes, we have shown that in cells normally using the K-SAM exon, the BEK exon is not used efficiently even in the absence of the K-SAM exon. This is because these cells apparently express a titratable repressor of BEK exon use. In cells normally using the BEK exon, the K-SAM exon is not used efficiently even in the absence of a functional BEK exon. Three purines in the K-SAM polypyrimidine tract are at least in part responsible for this, as their mutation to pyrimidines leads to efficient use of the K-SAM exon, while mutating the BEK polypyrimidine tract to include these purines stops BEK exon use.

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