Evidence map›Paper›PMID 34214491›Full record

ArticleDevelopmental cell2021

SUMO fosters assembly and functionality of the MutSγ complex to facilitate meiotic crossing over.

Wei He, Gerrik F Verhees, Nikhil Bhagwat, Ye Yang, Dhananjaya S Kulkarni, Zane Lombardo, Sudipta Lahiri, Pritha Roy, Jiaming Zhuo, Brian Dang and 8 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Developmental cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 13 citations in OpenAlex.

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  10. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    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

18 authors at 3 institutions in 1 country.

Wei HeHoward Hughes Medical Institute, University of California, Davis, Davis, CA, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Gerrik F VerheesDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Nikhil BhagwatHoward Hughes Medical Institute, University of California, Davis, Davis, CA, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Ye YangHoward Hughes Medical Institute, University of California, Davis, Davis, CA, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Dhananjaya S KulkarniHoward Hughes Medical Institute, University of California, Davis, Davis, CA, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Zane LombardoDepartment of Molecular Biology and Biochemistry, Molecular Biophysics Program, Wesleyan University, Middletown, CT, USA.
Sudipta LahiriDepartment of Molecular Biology and Biochemistry, Molecular Biophysics Program, Wesleyan University, Middletown, CT, USA.
Pritha RoyDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Jiaming ZhuoDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Brian DangDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Andriana SnyderDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Shashank ShastryDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Michael MoezpoorDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Lilly AlocozyDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Kathy Gyehyun LeeDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Daniel PainterDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA.
Ishita MukerjiDepartment of Molecular Biology and Biochemistry, Molecular Biophysics Program, Wesleyan University, Middletown, CT, USA.
Neil HunterHoward Hughes Medical Institute, University of California, Davis, Davis, CA, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, CA, USA. Electronic address: nhunter@ucdavis.edu.
University of California, Davis · USWesleyan University · USHoward Hughes Medical Institute · US

Funding

Joint Molecule Resolution During Meiotic RecombinationR01GM074223 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI HUNTER, NEIL · 2005 to 2025
$6.0M
Investigating the Role of MutSy in Meiotic Recombination and Maintaining Genome IntegrityR15GM135904 · NIGMS · WESLEYAN UNIVERSITY · PI MUKERJI, ISHITA · 2019 to 2019
$493k
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM074223NIGMS NIH HHS R15 GM135904
6 · The paper itself

Abstract

Crossing over is essential for chromosome segregation during meiosis. Protein modification by SUMO is implicated in crossover control, but pertinent targets have remained elusive. Here we identify Msh4 as a target of SUMO-mediated crossover regulation. Msh4 and Msh5 constitute the MutSγ complex, which stabilizes joint-molecule (JM) recombination intermediates and facilitates their resolution into crossovers. Msh4 SUMOylation enhances these processes to ensure that each chromosome pair acquires at least one crossover. Msh4 is directly targeted by E2 conjugase Ubc9, initially becoming mono-SUMOylated in response to DNA double-strand breaks, then multi/poly-SUMOylated forms arise as homologs fully engage. Mechanistically, SUMOylation fosters interaction between Msh4 and Msh5. We infer that initial SUMOylation of Msh4 enhances assembly of MutSγ in anticipation of JM formation, while secondary SUMOylation may promote downstream functions. Regulation of Msh4 by SUMO is distinct and independent of its previously described stabilization by phosphorylation, defining MutSγ as a hub for crossover control.

Indexed as

Crossing Over, GeneticMeiosisSumoylationCell NucleusChromosome SegregationDNADNA-Binding ProteinsDNA DamageDNA RepairSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9DNADNA-Binding ProteinsMSH4 protein, S cerevisiaeMSH5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9aneuploidychromosome segregationcrossing overDNA repairdouble-strand breakhomologous recombinationmeiosisMutSprotein modificationSUMO

Identifiers

PMID34214491
PMCPMC8319151
OpenAlexW3173912567

What OpenQuestion holds

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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.