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Redirecting SR Protein Nuclear Trafficking through an Allosteric Platform.

Brandon E Aubol1, Kendra L Hailey2, Laurent Fattet1

  • 1Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0636, USA.

Journal of Molecular Biology
|June 4, 2017
PubMed
Summary

Protein phosphatase 1 (PP1) interacts with serine-arginine (SR) protein splicing factor SRSF1. This interaction regulates SRSF1 phosphorylation, ensuring its proper nuclear localization and splicing function.

Keywords:
SR proteinkinasekineticsphosphatasephosphorylation

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Serine-arginine (SR) proteins are crucial for mRNA splicing.
  • Phosphorylation and dephosphorylation of SR proteins regulate their nuclear localization and function.
  • Opposing effects of these modifications on SR protein movement present a regulatory paradox.

Purpose of the Study:

  • To investigate the interaction between protein phosphatase 1 (PP1) and the SR protein splicing factor SRSF1.
  • To elucidate the mechanism balancing phosphorylation and dephosphorylation of SRSF1.
  • To understand the regulation of SR protein subnuclear localization.

Main Methods:

  • Biochemical assays to study protein-protein interactions.
  • In vitro and in-cell experiments to assess protein phosphorylation.
  • Analysis of SRSF1 subnuclear localization.

Main Results:

  • The RNA recognition motif 1 (RRM1) of SRSF1 binds to PP1.
  • PP1 binding to SRSF1's RRM1 allosterically represses PP1's catalytic activity.
  • Disruption of this interaction alters SRSF1 phosphorylation and nuclear distribution.

Conclusions:

  • An allosteric platform involving SRSF1 and PP1 balances SR protein phosphorylation levels.
  • This balance is critical for maintaining SR proteins in a "goldilocks" phosphorylation state for proper nuclear storage.
  • The findings resolve the paradox of opposing effects of phosphorylation and dephosphorylation on SR protein localization.