title: The Activity-Dependent Regulation of Protein Kinase Stability by the Localization to P-Bodies.
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.
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
authors.forename: Bo
authors.initials: B
authors.lastname: Zhang
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
authors.forename: Qian
authors.initials: Q
authors.lastname: Shi
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
authors.forename: Sapna N
authors.initials: SN
authors.lastname: Varia
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
authors.forename: Siyuan
authors.initials: S
authors.lastname: Xing
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
authors.forename: Bethany M
authors.initials: BM
authors.lastname: Klett
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
authors.forename: Laura A
authors.initials: LA
authors.lastname: Cook
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210 herman.81@osu.edu.
authors.forename: Paul K
authors.initials: PK
authors.lastname: Herman
mesh_terms: D047389:Casein Kinase I / Q000235:genetics* / Q000378:metabolism; D003593:Cytoplasm / Q000235:genetics / Q000378:metabolism; D003594:Cytoplasmic Granules / Q000235:genetics* / Q000378:metabolism; D004722:Endoribonucleases / Q000235:genetics* / Q000378:metabolism; D004795:Enzyme Stability / Q000235:genetics; D004926:Escherichia coli; D006367:HeLa Cells; D006801:Humans; D021381:Protein Transport / Q000235:genetics; D012261:Ribonucleoproteins / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics* / Q000378:metabolism; D013312:Stress, Physiological / Q000235:genetics
chemical_list: D012261:Ribonucleoproteins; D029701:Saccharomyces cerevisiae Proteins; D047389:Casein Kinase I; C070775:HRR25 protein, S cerevisiae; C400572:DCP2 protein, S cerevisiae; D004722:Endoribonucleases
keywords: Dcp2 decapping enzyme; casein kinase 1; processing bodies; protein kinase; protein stability; ribonucleoprotein granules