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.
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This work was supported by a grant from the National Institute of General Medical Sciences (R35GM130352) to EDR.
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Shattuck, J.E., Cascarina, S.M., Paul, K.R. et al. Sky1: at the intersection of prion-like proteins and stress granule regulation. Curr Genet 66, 463–468 (2020). https://doi.org/10.1007/s00294-019-01044-z
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DOI: https://doi.org/10.1007/s00294-019-01044-z