Evidence map›Paper›PMID 21070970›Full record

ArticleMolecular cell2010

Psh1 is an E3 ubiquitin ligase that targets the centromeric histone variant Cse4.

Geetha Hewawasam, Manjunatha Shivaraju, Mark Mattingly, Swaminathan Venkatesh, Skylar Martin-Brown, Laurence Florens, Jerry L Workman, Jennifer L Gerton

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
20.3field-weighted citation impact, top 1% 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

119 citing papers in PubMed, 169 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
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  15. SUMO control of centromere homeostasis.Frontiers in cell and developmental biology · 2023
    Review
  16. Histone modification inComputational and structural biotechnology journal · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

59 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 2 countries.

Geetha HewawasamStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Manjunatha Shivaraju
Mark Mattingly
Swaminathan Venkatesh
Skylar Martin-Brown
Laurence Florens
Jerry L Workman
Jennifer L Gerton
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 a variant of histone H3 that is incorporated into a single nucleosome at each centromere in budding yeast. We have discovered an E3 ubiquitin ligase, called Psh1, which controls the cellular level of Cse4 via ubiquitylation and proteolysis. The activity of Psh1 is dependent on both its RING and zinc finger domains. We demonstrate the specificity of the ubiquitylation activity of Psh1 toward Cse4 in vitro and map the sites of ubiquitylation. Mutation of key lysines prevents ubiquitylation of Cse4 by Psh1 in vitro and stabilizes Cse4 in vivo. While deletion of Psh1 stabilizes Cse4, elimination of the Cse4-specific chaperone Scm3 destabilizes Cse4, and the addition of Scm3 to the Psh1-Cse4 ubiquitylation reaction prevents Cse4 ubiquitylation, together suggesting Scm3 may protect Cse4 from ubiquitylation. Without Psh1, Cse4 overexpression is toxic and Cse4 is found at ectopic locations. Our results suggest Psh1 functions to prevent the mislocalization of Cse4.

Indexed as

CentromereChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene DeletionHistonesHumansPeptide Elongation FactorsProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProtein StabilityProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsHistonesPeptide Elongation FactorsProtein IsoformsPsh1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsScm3 protein, S cerevisiaeUbiquitin-Protein Ligases

Identifiers

PMID21070970
PMCPMC2998187
OpenAlexW1992906999

What OpenQuestion holds

Textmetadata
LicenceTDM
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.