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

Overview

Journal Genetics

Publisher Oxford University Press

Specialty Genetics

Date 2016 May 17

PMID 27182950

Citations 16

Authors

Bo Zhang

Qian Shi

Sapna N Varia

Siyuan Xing

Bethany M Klett

Laura A Cook

Paul K Herman

Affiliations

Soon will be listed here.

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.

Citing Articles

Casein Kinase I Protein Hrr25 Is Required for Pin4 Phosphorylation and Mediates Cell Wall Integrity Signaling in .

Bhattarai A, Bhondeley M, Liu Z Genes (Basel). 2025; 16(1.

PMID: 39858641 PMC: 11765155. DOI: 10.3390/genes16010094.

Parallel Nonfunctionalization of CK1δ/ε Kinase Ohnologs Following a Whole-Genome Duplication Event.

Evans-Yamamoto D, Dube A, Saha G, Plante S, Bradley D, Gagnon-Arsenault I Mol Biol Evol. 2023; 40(12).

PMID: 37979156 PMC: 10699747. DOI: 10.1093/molbev/msad246.

Parallel nonfunctionalization of CK1δ/ε kinase ohnologs following a whole-genome duplication event.

Evans-Yamamoto D, Dube A, Saha G, Plante S, Bradley D, Gagnon-Arsenault I bioRxiv. 2023; .

PMID: 37873368 PMC: 10592909. DOI: 10.1101/2023.10.02.560513.

Quantitative reconstitution of yeast RNA processing bodies.

Currie S, Xing W, Muhlrad D, Decker C, Parker R, Rosen M Proc Natl Acad Sci U S A. 2023; 120(14):e2214064120.

PMID: 36972455 PMC: 10083542. DOI: 10.1073/pnas.2214064120.

A distinct P-body-like granule is induced in response to the disruption of microtubule integrity in Saccharomyces cerevisiae.

Hurst Z, Liu W, Shi Q, Herman P Genetics. 2022; 222(1).

PMID: 35876801 PMC: 9434292. DOI: 10.1093/genetics/iyac105.

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