The Drosophila Splicing Factor PSI Is Phosphorylated by Casein Kinase II and Tousled-Like Kinase |
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| Authors: | J Matthew Taliaferro Dhruv Marwha Julie L Aspden Daniela Mavrici Nathalie E Cheng Lori A Kohlstaedt Donald C Rio |
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| Institution: | 1. Department of Molecular and Cell Biology, University of California, Berkeley, California, United States of America.; 2. Center for Integrative Genomics, University of California, Berkeley, California, United States of America.; 3. California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, California, United States of America.; International Centre for Genetic Engineering and Biotechnology, Italy, |
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| 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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