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

  • Author(s): Taliaferro, J
  • Marwha, Dhruv
  • Aspden, Julie
  • Mavrici, Daniela
  • Cheng, Nathalie
  • Kohlstaedt, Lori
  • RIO, Donald C.
  • et al.
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.

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