Evidence map›Paper›PMID 27182950›Full record

ArticleGenetics2016

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

Bo Zhang, Qian Shi, Sapna N Varia, Siyuan Xing, Bethany M Klett, Laura A Cook, Paul K Herman

Abstract read
In one paragraph

Article in Genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Article
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  5. Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Bo ZhangDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
Qian ShiDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
Sapna N VariaDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
Siyuan XingDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
Bethany M KlettDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
Laura A CookDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210.
Paul K HermanDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210 herman.81@osu.edu.

Funding

The regulation of autophagy pathways in eukaryotic cellsR01GM065227 · NIGMS · OHIO STATE UNIVERSITY · PI HERMAN, PAUL K · 2002 to 2014
$3.6M
The regulation and function of cytoplasmic foci in quiescent cellsR01GM101191 · NIGMS · OHIO STATE UNIVERSITY · PI HERMAN, PAUL K · 2013 to 2016
$1.2M
NIGMS NIH HHS R01 GM065227NIGMS NIH HHS R01 GM101191
6 · The paper itself

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.

Indexed as

Casein Kinase ICytoplasmCytoplasmic GranulesEndoribonucleasesEnzyme StabilityEscherichia coliHeLa CellsHumansProtein TransportRibonucleoproteinsSaccharomyces cerevisiae ProteinsStress, PhysiologicalCasein Kinase IDCP2 protein, S cerevisiaeEndoribonucleasesHRR25 protein, S cerevisiaeRibonucleoproteinsSaccharomyces cerevisiae Proteinscasein kinase 1Dcp2 decapping enzymeprocessing bodiesprotein kinaseprotein stabilityribonucleoprotein granules

Identifiers

PMID27182950
PMCPMC4937477

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.