Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 429, Issue 14, Pages 2178-2191Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2017.05.022
Keywords
kinase; kinetics; phosphorylation; phosphatase; SR protein
Categories
Funding
- NIH [GM67969, GM95828]
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Although phosphorylation directs serine-arginine (SR) proteins from nuclear storage speckles to the nucleoplasm for splicing function, dephosphorylation paradoxically induces similar movement, raising the question of how such chemical modifications are balanced in these essential splicing factors. In this new study, we investigated the interaction of protein phosphatase 1 (PP1) with the SR protein splicing factor (SRSF1) to understand the foundation of these opposing effects in the nucleus. We found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism. Disruption of RRM1-PP1 interactions reduces the phosphorylation status of the RS domain in vitro and in cells, redirecting SRSF1 in the nucleus. The data imply that an allosteric SR protein-phosphatase platform balances phosphorylation levels in a goldilocks region for the proper subnuclear storage of an SR protein splicing factor. (C) 2017 Elsevier Ltd. All rights reserved.
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