The Drosophila splicing factor PSI is phosphorylated by casein kinase II and tousled-like kinase.
- Author(s): Taliaferro, J Matthew;
- Marwha, Dhruv;
- Aspden, Julie L;
- Mavrici, Daniela;
- Cheng, Nathalie E;
- Kohlstaedt, Lori A;
- Rio, Donald C
- Editor(s): Buratti, Emanuele
- et al.
Published Web Locationhttps://doi.org/10.1371/journal.pone.0056401
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.