The Activity-Dependent Regulation of Protein Kinase Stability by the Localization to P-Bodies.

Autor:	Zhang B; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210., Shi Q; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210., Varia SN; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210., Xing S; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210., Klett BM; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210., Cook LA; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210., Herman PK; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210 herman.81@osu.edu.
Jazyk:	angličtina
Zdroj:	Genetics [Genetics] 2016 Jul; Vol. 203 (3), pp. 1191-202. Date of Electronic Publication: 2016 May 06.
DOI:	10.1534/genetics.116.187419
Abstrakt:	The eukaryotic cytoplasm contains a variety of ribonucleoprotein (RNP) granules in addition to the better-understood membrane-bound organelles. These granules form in response to specific stress conditions and contain a number of signaling molecules important for the control of cell growth and survival. However, relatively little is known about the mechanisms responsible for, and the ultimate consequences of, this protein localization. Here, we show that the Hrr25/CK1δ protein kinase is recruited to cytoplasmic processing bodies (P-bodies) in an evolutionarily conserved manner. This recruitment requires Hrr25 kinase activity and the Dcp2 decapping enzyme, a core constituent of these RNP granules. Interestingly, the data indicate that this localization sequesters active Hrr25 away from the remainder of the cytoplasm and thereby shields this enzyme from the degradation machinery during these periods of stress. Altogether, this work illustrates how the presence within an RNP granule can alter the ultimate fate of the localized protein. (Copyright © 2016 by the Genetics Society of America.)
Databáze:	MEDLINE
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