Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1939304 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
Dok adapter proteins have been primarily implicated in negative regulation of tyrosine kinase signaling, but Dok-4 has been reported to exert both inhibitory and stimulatory effects. We have identified a splice variant of Dok-4, Dok-4b, which contains a 39 aa insert within the its C-terminal region. The â¼45Â kDa Dok-4b protein was detected in several human epithelial cell lines. Based on genomic sequences, Dok-4b was also predicted to exist in primates and possibly bovines, but not in rodents or other species. Compared to Dok-4, Dok-4b inhibited the tyrosine kinase-induced activation of both Erk and Elk-1 more strongly. Truncation of the C-terminal region of Dok-4 (Dok-4 ÎCT) also enhanced the inhibitory activity of Dok-4, whereas expression of the isolated C-terminal domain enhanced Elk-1 activation, suggesting that the N-terminus and C-terminus of Dok-4 possess opposing inhibitory and stimulatory properties, respectively, the balance of which is altered by alternative splicing of Dok-4 to Dok-b.
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Authors
Cindy Baldwin, Arda Bedirian, Hongping Li, Tomoko Takano, Serge Lemay,