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- W1531644439 abstract "Mammalian Clk/Sty is the prototype for a family of dual specificity kinases (termed LAMMER kinases) that have been conserved in evolution, but whose physiological substrates are unknown. In a yeast two-hybrid screen, the Clk/Sty kinase specifically interacted with RNA binding proteins, particularly members of the serine/arginine-rich (SR) family of splicing factors. Clk/Sty itself has an serine/arginine-rich non-catalytic N-terminal region which is important for its association with SR splicing factors. In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Tryptic phosphopeptide mapping demonstrated that the sites on ASF/SF2 phosphorylated in vitro overlap with those phosphorylated in vivo. Immunofluorescence studies showed that a catalytically inactive form of Clk/Sty co-localized with SR proteins in nuclear speckles. Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors." @default.
- W1531644439 created "2016-06-24" @default.
- W1531644439 creator A5033568530 @default.
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- W1531644439 creator A5081242070 @default.
- W1531644439 creator A5087452652 @default.
- W1531644439 date "1996-01-01" @default.
- W1531644439 modified "2023-10-12" @default.
- W1531644439 title "The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution." @default.
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- W1531644439 doi "https://doi.org/10.1002/j.1460-2075.1996.tb00357.x" @default.
- W1531644439 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/449941" @default.
- W1531644439 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8617202" @default.
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