Evidence map›Paper›PMID 21444718›Full record

ArticleMolecular and cellular biology2011

DNA repair and global sumoylation are regulated by distinct Ubc9 noncovalent complexes.

John Prudden, J Jefferson P Perry, Minghua Nie, Ajay A Vashisht, Andrew S Arvai, Chiharu Hitomi, Grant Guenther, James A Wohlschlegel, John A Tainer, Michael N Boddy

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

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3 · Its place in the literature

Who cites it

39 citing papers in PubMed.

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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

10 authors.

John PruddenDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
J Jefferson P Perry
Minghua Nie
Ajay A Vashisht
Andrew S Arvai
Chiharu Hitomi
Grant Guenther
James A Wohlschlegel
John A Tainer
Michael N Boddy

Funding

Studies of the Rad60-Smc5-Smc6 DNA Repair ComplexR01GM068608 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BODDY, MICHAEL N · 2003 to 2020
$6.2M
Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
SUMO-dependent Regulation of Ubiquitin Ligases in Genomic StabilityR01GM081840 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BODDY, MICHAEL N · 2009 to 2018
$3.0M
NIGMS NIH HHS GM068608NIGMS NIH HHS GM081840NIGMS NIH HHS GM089778NIGMS NIH HHS R01 GM068608NIGMS NIH HHS R01 GM081840NIGMS NIH HHS R01 GM089778
6 · The paper itself

Abstract

Global sumoylation, SUMO chain formation, and genome stabilization are all outputs generated by a limited repertoire of enzymes. Mechanisms driving selectivity for each of these processes are largely uncharacterized. Here, through crystallographic analyses we show that the SUMO E2 Ubc9 forms a noncovalent complex with a SUMO-like domain of Rad60 (SLD2). Ubc9:SLD2 and Ubc9:SUMO noncovalent complexes are structurally analogous, suggesting that differential recruitment of Ubc9 by SUMO or Rad60 provides a novel means for such selectivity. Indeed, deconvoluting Ubc9 function by disrupting either the Ubc9:SLD2 or Ubc9:SUMO noncovalent complex reveals distinct roles in facilitating sumoylation. Ubc9:SLD2 acts in the Nse2 SUMO E3 ligase-dependent pathway for DNA repair, whereas Ubc9:SUMO instead promotes global sumoylation and chain formation, via the Pli1 E3 SUMO ligase. Moreover, this Pli1-dependent SUMO chain formation causes the genome instability phenotypes of SUMO-targeted ubiquitin ligase (STUbL) mutants. Overall, we determine that, unexpectedly, Ubc9 noncovalent partner choice dictates the role of sumoylation in distinct cellular pathways.

Indexed as

DNA RepairBlotting, WesternCarrier ProteinsChromosomal Proteins, Non-HistoneCrystallography, X-RayHumansMass SpectrometryModels, MolecularMutationProtein Structure, QuaternarySchizosaccharomycesSchizosaccharomyces pombe ProteinsSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Carrier ProteinsChromosomal Proteins, Non-HistoneNFATC2IP protein, humanNse2 protein, S pombeRad60 protein, S pombeSchizosaccharomyces pombe ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID21444718
PMCPMC3133251

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.