Evidence map›Paper›PMID 32130890›Full record

ArticleMolecular cell2020

Regulated Proteolysis of MutSγ Controls Meiotic Crossing Over.

Wei He, H B D Prasada Rao, Shangming Tang, Nikhil Bhagwat, Dhananjaya S Kulkarni, Yunmei Ma, Maria A W Chang, Christie Hall, Junxi Wang Bragg, Harrison S Manasca and 7 more

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

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

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  14. RNF212B E3 ligase is essential for crossover designation and maturation during male and female meiosis in the mouse.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

17 authors at 4 institutions in 2 countries.

Wei HeHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
H B D Prasada RaoHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Shangming TangHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Nikhil BhagwatHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Dhananjaya S KulkarniHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Yunmei MaHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Maria A W ChangDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Christie HallDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Junxi Wang BraggDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Harrison S ManascaDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Christa BakerDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Gerrik F VerheesDepartment of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA.
Lepakshi RanjhaInstitute for Research in Biomedicine, Università della Svizzera italiana, Bellinzona, Switzerland.
Xiangyu ChenDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA.
Nancy M HollingsworthDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA.
Petr CejkaInstitute for Research in Biomedicine, Università della Svizzera italiana, Bellinzona, Switzerland.
Neil HunterHoward Hughes Medical Institute, University of California, Davis, Davis, California, USA; Department of Microbiology & Molecular Genetics, University of California, Davis, Davis, California, USA; Department of Molecular & Cellular Biology, University of California, Davis, Davis, California, USA; Department of Cell Biology & Human Anatomy, University of California, Davis, Davis, California, USA. Electronic address: nhunter@ucdavis.edu.
University of California, Davis · USHoward Hughes Medical Institute · USStony Brook University · USUniversità della Svizzera italiana · CH

Funding

ANALYSIS OF MEIOTIC CHROMOSOME SYNAPSIS IN YEASTR01GM050717 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI HOLLINGSWORTH, NANCY M. · 1995 to 2020
$8.0M
Joint Molecule Resolution During Meiotic RecombinationR01GM074223 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI HUNTER, NEIL · 2005 to 2025
$6.0M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM050717NIGMS NIH HHS R01 GM074223
6 · The paper itself

Abstract

Crossover recombination is essential for accurate chromosome segregation during meiosis. The MutSγ complex, Msh4-Msh5, facilitates crossing over by binding and stabilizing nascent recombination intermediates. We show that these activities are governed by regulated proteolysis. MutSγ is initially inactive for crossing over due to an N-terminal degron on Msh4 that renders it unstable by directly targeting proteasomal degradation. Activation of MutSγ requires the Dbf4-dependent kinase Cdc7 (DDK), which directly phosphorylates and thereby neutralizes the Msh4 degron. Genetic requirements for Msh4 phosphorylation indicate that DDK targets MutSγ only after it has bound to nascent joint molecules (JMs) in the context of synapsing chromosomes. Overexpression studies confirm that the steady-state level of Msh4, not phosphorylation per se, is the critical determinant for crossing over. At the DNA level, Msh4 phosphorylation enables the formation and crossover-biased resolution of double-Holliday Junction intermediates. Our study establishes regulated protein degradation as a fundamental mechanism underlying meiotic crossing over.

Indexed as

Crossing Over, GeneticCell Cycle ProteinsChromosome PairingDNA-Binding ProteinsMeiosisPhosphorylationProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesProteolysisSaccharomyces cerevisiae ProteinsCDC7 protein, S cerevisiaeCell Cycle ProteinsDNA-Binding ProteinsMSH4 protein, S cerevisiaeProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsaneuploidyCdc7chromosomecrossing overdegronHolliday Junctionhomologous recombinationmeiosisMutSproteasome

Identifiers

PMID32130890
PMCPMC7289160
OpenAlexW3010116705

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.