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

ABSTRACT: 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.

SUBMITTER: Taliaferro JM

PROVIDER: S-EPMC3577899 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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

Taliaferro J Matthew JM Marwha Dhruv D Aspden Julie L JL Mavrici Daniela D Cheng Nathalie E NE Kohlstaedt Lori A LA Rio Donald C DC

PloS one 20130220 2

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 ...[more]

PMID: 23437125

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