The Drosophila splicing factor PSI is phosphorylated by casein kinase II and tousled-like kinase.

J Matthew Taliaferro, Dhruv Marwha, Julie L Aspden, Daniela Mavrici, Nathalie E Cheng, Lori A Kohlstaedt, Donald C Rio

PloS one 2013

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Alternative splicing of pre-mRNA is a highly regulated process that allows cells to change their genetic informational output. These changes are mediated by protein factors that directly bind specific pre-mRNA sequences. Although much is known about how these splicing factors regulate pre-mRNA splicing events, comparatively little is known about the regulation of the splicing factors themselves. Here, we show that the Drosophila splicing factor P element Somatic Inhibitor (PSI) is phosphorylated at at least two different sites by at minimum two different kinases, casein kinase II (CK II) and tousled-like kinase (tlk). These phosphorylation events may be important for regulating protein-protein interactions involving PSI. Additionally, we show that PSI interacts with several proteins in Drosophila S2 tissue culture cells, the majority of which are splicing factors.

Citation

J Matthew Taliaferro, Dhruv Marwha, Julie L Aspden, Daniela Mavrici, Nathalie E Cheng, Lori A Kohlstaedt, Donald C Rio. The Drosophila splicing factor PSI is phosphorylated by casein kinase II and tousled-like kinase. PloS one. 2013;8(2):e56401