Evidence map›Paper›PMID 23935535›Full record

ArticlePLoS genetics2013

Distinct SUMO ligases cooperate with Esc2 and Slx5 to suppress duplication-mediated genome rearrangements.

Claudio P Albuquerque, Guoliang Wang, Nancy S Lee, Richard D Kolodner, Christopher D Putnam, Huilin Zhou

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 78 citations in OpenAlex.

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Claudio P AlbuquerqueLudwig Institute for Cancer Research, University of California School of Medicine, San Diego, La Jolla, CA, USA.
Guoliang Wang
Nancy S Lee
Richard D Kolodner
Christopher D Putnam
Huilin Zhou
Ludwig Cancer Research · US

Funding

SYNTHETIC SYSTEMSP50GM085764 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HASTY, JEFF M, IDEKER, TREY · 2010 to 2018
$23.3M
ENZYMATIC MECHANISMS OF GENETIC RECOMBINATIONR01GM026017 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Richard D Kolodner · 1985 to 2026
$10.5M
Regulation and functions of DNA damage checkpoint kinases in YeastR01GM080469 · NIGMS · LUDWIG INSTITUTE FOR CANCER RES LTD · PI ZHOU, HUILIN · 2007 to 2011
$1.4M
ENZYMATIC MECHANISMS OF GENETIC RECOMBINATIONR37GM026017 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI KOLODNER, RICHARD D · 1992 to 2001
$759k
NIGMS NIH HHS GM080469NIGMS NIH HHS GM085764NIGMS NIH HHS GM26017NIGMS NIH HHS P50 GM085764NIGMS NIH HHS R01 GM026017NIGMS NIH HHS R01 GM080469NIGMS NIH HHS R37 GM026017
6 · The paper itself

Abstract

Suppression of duplication-mediated gross chromosomal rearrangements (GCRs) is essential to maintain genome integrity in eukaryotes. Here we report that SUMO ligase Mms21 has a strong role in suppressing GCRs in Saccharomyces cerevisiae, while Siz1 and Siz2 have weaker and partially redundant roles. Understanding the functions of these enzymes has been hampered by a paucity of knowledge of their substrate specificity in vivo. Using a new quantitative SUMO-proteomics technology, we found that Siz1 and Siz2 redundantly control the abundances of most sumoylated substrates, while Mms21 more specifically regulates sumoylation of RNA polymerase-I and the SMC-family proteins. Interestingly, Esc2, a SUMO-like domain-containing protein, specifically promotes the accumulation of sumoylated Mms21-specific substrates and functions with Mms21 to suppress GCRs. On the other hand, the Slx5-Slx8 complex, a SUMO-targeted ubiquitin ligase, suppresses the accumulation of sumoylated Mms21-specific substrates. Thus, distinct SUMO ligases work in concert with Esc2 and Slx5-Slx8 to control substrate specificity and sumoylation homeostasis to prevent GCRs.

Indexed as

Cell Cycle ProteinsGene DuplicationGenome, FungalGenomic InstabilityLigasesNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificitySUMO-1 ProteinSumoylationUbiquitin-Protein LigasesCell Cycle ProteinsEsc2 protein, S cerevisiaeLigasesMms21 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae ProteinsSiz1 protein, S cerevisiaeSiz2 protein, S cerevisiaeSlx5 protein, S cerevisiaeSUMO-1 ProteinUbiquitin-Protein Ligases

Identifiers

PMID23935535
PMCPMC3731205
OpenAlexW2073869348

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.