Evidence map›Paper›PMID 25183013›Full record

ArticleThe Journal of biological chemistry2014

Phosphorylation by casein kinase 2 facilitates Psh1 protein-assisted degradation of Cse4 protein.

Geetha S Hewawasam, Mark Mattingly, Swaminathan Venkatesh, Ying Zhang, Laurence Florens, Jerry L Workman, Jennifer L Gerton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
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

21 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. SUMO control of centromere homeostasis.Frontiers in cell and developmental biology · 2023
    Review
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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 at 1 institution in 1 country.

Geetha S HewawasamFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and.
Mark MattinglyFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and.
Swaminathan VenkateshFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and.
Ying ZhangFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and.
Laurence FlorensFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and.
Jerry L WorkmanFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and.
Jennifer L GertonFrom the Stowers Institute for Medical Research, Kansas City, Missouri 64110 and Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66160 jeg@stowers.org.
Stowers Institute for Medical Research · US

Funding

Molecular Mechanisms of Chromosome Segregation in YeastR01GM080477 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI GERTON, JENNIFER L · 2008 to 2012
$1.5M
NIGMS NIH HHS R01 GM080477NIGMS NIH HHS R01GM080477
6 · The paper itself

Abstract

Cse4 is the centromeric histone H3 variant in budding yeast. Psh1 is an E3 ubiquitin ligase that controls Cse4 levels through proteolysis. Here we report that Psh1 is phosphorylated by the Cka2 subunit of casein kinase 2 (CK2) to promote its E3 activity for Cse4. Deletion of CKA2 significantly stabilized Cse4. Consistent with phosphorylation promoting the activity of Psh1, Cse4 was stabilized in a Psh1 phosphodepleted mutant strain in which the major phosphorylation sites were changed to alanines. Phosphorylation of Psh1 did not control Psh1-Cse4 or Psh1-Ubc3(E2) interactions. Although Cse4 was highly stabilized in a cka2Δ strain, mislocalization of Cse4 was mild, suggesting that Cse4 misincorporation was prevented by the intact Psh1-Cse4 association. Supporting this idea, Psh1 was also stabilized in a cka2Δ strain. Collectively our data suggest that phosphorylation is crucial in Psh1-assisted control of Cse4 levels and that the Psh1-Cse4 association itself functions to prevent Cse4 misincorporation.

Indexed as

Casein Kinase IICatalysisCentromereChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene DeletionKinetochoresPeptide Elongation FactorsPhosphorylationProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein LigasesCasein Kinase IIChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsPeptide Elongation FactorsProteasome Endopeptidase ComplexPsh1 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein LigasesCentromereCK2Cse4/CENP-AE3 Ubiquitin LigasePhosphorylationProteolysisPsh1Yeast

Identifiers

PMID25183013
PMCPMC4200280
OpenAlexW2058505738

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.