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10.1534/genetics.116.187419

http://scihub22266oqcxt.onion/10.1534/genetics.116.187419
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C4937477!4937477!27182950
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suck abstract from ncbi


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pmid27182950      Genetics 2016 ; 203 (3): 1191-202
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  • The Activity-Dependent Regulation of Protein Kinase Stability by the Localization to P-Bodies #MMPMID27182950
  • Zhang B; Shi Q; Varia SN; Xing S; Klett BM; Cook LA; Herman PK
  • Genetics 2016[Jul]; 203 (3): 1191-202 PMID27182950show ga
  • 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/CK1? 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.
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