| Literature DB >> 31745569 |
Jenifer E Shattuck1, Sean M Cascarina1, Kacy R Paul1, Eric D Ross2.
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.Entities:
Keywords: Kinase; Prion-like; Protein aggregation; Stress granule
Mesh:
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Year: 2019 PMID: 31745569 PMCID: PMC7493465 DOI: 10.1007/s00294-019-01044-z
Source DB: PubMed Journal: Curr Genet ISSN: 0172-8083 Impact factor: 3.886