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The DUSP domain of pseudophosphatase MK-STYX interacts with G3BP1 to decrease stress granules.

Jonathan Smailys1, Fei Jiang1, Tatiana Prioleau1

  • 1Department of Biology, Integrated Science Center, William and Mary, Williamsburg, VA, 23185, USA.

Archives of Biochemistry and Biophysics
|July 29, 2023
PubMed
Summary

Mitogen activated protein kinase phosphoserine/threonine/tyrosine-binding protein (MK-STYX) reduces stress granules by interacting with G3BP1. Its DUSP domain decreases G3BP1 tyrosine phosphorylation, inhibiting stress granule formation.

Keywords:
Cell division cycle 25 phosphatase homology 2Dual specificity domainG3BP1MK-STYXProtein tyrosine phosphatasePseudophosphataseStress granules

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitogen activated protein kinase phosphoserine/threonine/tyrosine-binding protein (MK-STYX) is a pseudophosphatase.
  • MK-STYX interacts with G3BP1 (Ras-GAP SH3 domain-binding-1) and modulates stress granules.
  • Stress granules are stalled mRNA aggregates implicated in cellular stress responses.

Purpose of the Study:

  • To elucidate the mechanism by which MK-STYX reduces stress granules.
  • To investigate the roles of MK-STYX's truncated domains (CH2 and DUSP) in stress granule regulation.
  • To analyze the interaction between MK-STYX domains and G3BP1.

Main Methods:

  • Utilized truncated MK-STYX domains (CH2 and DUSP) in cellular assays.
  • Induced stress granules using sodium arsenite in HEK/293 and HeLa cells.
  • Performed co-immunoprecipitation experiments to assess protein interactions.
  • Monitored G3BP1 tyrosine phosphorylation levels.

Main Results:

  • Wild-type MK-STYX and its DUSP domain significantly decreased stress granules.
  • The DUSP domain of MK-STYX interacted with G3BP1 and decreased G3BP1 tyrosine phosphorylation.
  • The CH2 domain of MK-STYX increased stress granule formation and G3BP1 tyrosine phosphorylation.
  • MK-STYX's DUSP domain negatively altered G3BP1 tyrosine phosphorylation, reducing stress granules.

Conclusions:

  • MK-STYX decreases G3BP1-induced stress granules through its DUSP domain.
  • The DUSP domain's interaction with G3BP1 and subsequent reduction in tyrosine phosphorylation is key to inhibiting stress granule formation.
  • The CH2 domain appears to have an opposing role, promoting stress granule formation.