| Autor: |
GARCÍA-SACRISTÁN, Ana, FERNÁNDEZ-NESTOSA, María J, HERNÁNDEZ, Pablo, SCHVARTZMAN, Jorge B, KRIMER, Dora B |
| Zdroj: |
Cell Research; July 2005, Vol. 15 Issue: 7 p495-503, 9p |
| Abstrakt: |
ABSTRACTClk/STY is a LAMMER protein kinase capable to phosphorylate serine/arginine-rich (SR) proteins that modulate prem-RNA splicing. Clk/STY alternative splicing generates transcripts encoding a full-length kinase and a truncated catalytically inactive protein. Here we showed that clk/STY, as well as other members of the family (e.g. clk2, clk3 and clk4), are up-regulated during HMBA-induced erythroleukemia cell differentiation. mRNAs coding for the full-length and the truncated forms were responsible for the overall increased expression. In clk/STY, however, a switch was observed for the ratio of the two alternative spliced products. In undifferentiated cells the full-length transcript was more abundant whereas the transcript encoding for the truncated form predominated at latter stages of differentiation. Surprisingly, overexpression of clk/STY did not alter the splicing switch upon differentiation in MEL cells. These results suggest that clk/STY might contribute to control erythroid differentiation by a mechanism that implicates a balance between these two isoforms. |
| Databáze: |
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