Sky1: at the intersection of prion-like proteins and stress granule regulation

Curr Genet. 2020 Jun;66(3):463-468. doi: 10.1007/s00294-019-01044-z. Epub 2019 Nov 19.

Abstract

Serine-arginine (SR) protein kinases regulate diverse cellular activities, including various steps in RNA maturation and transport. The yeast Saccharomyces cerevisiae expresses a single SR kinase, Sky1. Sky1 has a bipartite kinase domain, separated by an aggregation-prone prion-like domain (PrLD). The assembly of PrLDs is involved in the formation of various membraneless organelles, including stress granules; stress granules are reversible ribonucleoprotein assemblies that form in response to a variety of stresses. Here, we review a recent study suggesting that Sky1's PrLD promotes Sky1 recruitment to stress granules, and that Sky1 regulates stress granule dissolution by phosphorylating the RNA-shuttling protein Npl3.

Keywords: Kinase; Prion-like; Protein aggregation; Stress granule.

Publication types

  • Review

MeSH terms

  • Cytoplasmic Granules / metabolism*
  • Organelles / metabolism*
  • Phosphorylation
  • Prions / metabolism*
  • Protein Serine-Threonine Kinases / metabolism*
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Prions
  • Saccharomyces cerevisiae Proteins
  • SKY1 protein, S cerevisiae
  • Protein Serine-Threonine Kinases