Phosphoproteomics links glycogen synthase kinase-3 to RNA splicing

J Biol Chem. 2017 Nov 3;292(44):18256-18257. doi: 10.1074/jbc.H117.813527.

Abstract

Protein kinases play essential biological roles by phosphorylating a diverse range of signaling molecules, but deciphering their direct physiological targets remains a challenge. A new study by Shinde et al. uses phosphoproteomics to identify glycogen synthase kinase-3 (GSK-3) substrates in mouse embryonic stem cells (mESCs), providing a broad profile of GSK-3 activity and defining a new role for this central kinase in regulating RNA splicing.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing
  • Animals
  • Cell Cycle Proteins / metabolism
  • Embryonic Stem Cells / enzymology
  • Embryonic Stem Cells / metabolism
  • Gene Knockdown Techniques
  • Gene Ontology
  • Glycogen Synthase Kinase 3 / genetics
  • Glycogen Synthase Kinase 3 / metabolism*
  • Humans
  • Phosphorylation
  • Protein Processing, Post-Translational
  • RNA Splicing*
  • Substrate Specificity
  • Transcription Factors / metabolism*

Substances

  • Cell Cycle Proteins
  • Transcription Factors
  • Glycogen Synthase Kinase 3