Abstract：
: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.
journal_name
Geneticsjournal_title
Geneticsauthors
Zhang B,Shi Q,Varia SN,Xing S,Klett BM,Cook LA,Herman PKdoi
10.1534/genetics.116.187419subject
Has Abstractpub_date
2016-07-01 00:00:00pages
1191-202issue
3eissn
0016-6731issn
1943-2631pii
genetics.116.187419journal_volume
203pub_type
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