Evidence map›Paper›PMID 22593213›Full record

ArticleMolecular biology of the cell2012

Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization.

Suman Ghosh, Jennifer M Gardner, Christine J Smoyer, Jennifer M Friederichs, Jay R Unruh, Brian D Slaughter, Richard Alexander, Robert D Chisholm, Kenneth K Lee, Jerry L Workman and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. 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
1.7field-weighted citation impact, top 17% 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, 31 citations in OpenAlex.

  1. Review
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  12. Review
  13. Building a KATalogue of acetyllysine targeting and function.Briefings in functional genomics · 2016
    Review
  14. Article
  15. Review
  16. Article
  17. Cohesion promotes nucleolar structure and function.Molecular biology of the cell · 2014
    Article
  18. Article
  19. Review
  20. Article
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

11 authors at 1 institution in 1 country.

Suman GhoshStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Jennifer M Gardner
Christine J Smoyer
Jennifer M Friederichs
Jay R Unruh
Brian D Slaughter
Richard Alexander
Robert D Chisholm
Kenneth K Lee
Jerry L Workman
Sue L Jaspersen
Stowers Institute for Medical Research · US

Funding

MECHANISMS OF TRANSCRIPTIONAL REGULATION IN CHROMATINR01GM047867 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI WORKMAN, JERRY L · 1992 to 2014
$1.5M
NIGMS NIH HHS R01 GM047867
6 · The paper itself

Abstract

The Saccharomyces cerevisiae SUN-domain protein Mps3 is required for duplication of the yeast centrosome-equivalent organelle, the spindle pole body (SPB), and it is involved in multiple aspects of nuclear organization, including telomere tethering and gene silencing at the nuclear membrane, establishment of sister chromatid cohesion, and repair of certain types of persistent DNA double-stranded breaks. How these diverse SUN protein functions are regulated is unknown. Here we show that the Mps3 N-terminus is a substrate for the acetyltransferase Eco1/Ctf7 in vitro and in vivo and map the sites of acetylation to three lysine residues adjacent to the Mps3 transmembrane domain. Mutation of these residues shows that acetylation is not essential for growth, SPB duplication, or distribution in the nuclear membrane. However, analysis of nonacetylatable mps3 mutants shows that this modification is required for accurate sister chromatid cohesion and for chromosome recruitment to the nuclear membrane. Acetylation of Mps3 by Eco1 is one of the few regulatory mechanisms known to control nuclear organization.

Indexed as

Protein Processing, Post-TranslationalAcetylationAcetyltransferasesAmino Acid SequenceCell NucleusChromatidsDNA RepairLysineMembrane ProteinsMitosisMolecular Sequence DataNuclear ProteinsProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcetyltransferasesECO1 protein, S cerevisiaeLysineMembrane ProteinsMps3 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22593213
PMCPMC3386218
OpenAlexW2172244027

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.