Evidence map›Paper›PMID 42284145›Full record

ArticleCell reports2026

Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.

Rahel Wettstein, Grant A King, Adrian Henggeler, Madison E Walsh, Cyrus T Ruediger, Elçin Ünal, Joao Matos

Abstract read
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In one paragraph

Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Rahel WettsteinMax Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria; University of Vienna, Vienna, Austria; Institute of Biochemistry, ETH Zürich, 8093 Zürich, Switzerland.
Grant A KingDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Adrian HenggelerMax Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria; University of Vienna, Vienna, Austria; Institute of Biochemistry, ETH Zürich, 8093 Zürich, Switzerland.
Madison E WalshDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Cyrus T RuedigerDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Elçin ÜnalDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA 94720, USA; Center for Computational Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Electronic address: elcin@berkeley.edu.
Joao MatosMax Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria; University of Vienna, Vienna, Austria; Institute of Biochemistry, ETH Zürich, 8093 Zürich, Switzerland. Electronic address: joao.matos@maxperutzlabs.ac.at.

Funding

Elucidating Cellular Aging and Quality Control Pathways through Meiotic DifferentiationR01AG071801 · NIA · UNIVERSITY OF CALIFORNIA BERKELEY · PI UNAL, ELCIN · 2021 to 2025
$1.9M
NIA NIH HHS R01 AG071801
6 · The paper itself

Abstract

The nuclear pore complex (NPC) basket has been implicated in regulating meiotic recombination, but the underlying mechanism remained elusive. Here, we show that most basket subunits are required for controlled crossing-over in budding yeast. Central to this function, the nucleoporin Nup60 anchors the SUMO protease Ulp1 at the nuclear periphery, thereby protecting the synaptonemal complex (SC) protein Ecm11 from premature deSUMOylation. Unscheduled dissociation of Ulp1 from the NPC impairs Ecm11 SUMOylation, disrupts synapsis, elevates crossovers, and compromises gamete viability. Remarkably, engineered tethering of Ulp1 to the NPC restores SC integrity and recombination control in basket mutants. We further show that Polo-like kinase Cdc5 remodels SUMO homeostasis at the prophase I-metaphase I transition, triggering partial Ulp1 release from the NPC and phosphorylating the SUMO ligases Siz1 and Siz2. These findings uncover how nucleoporins, SUMO enzymes, and kinase signaling cooperate to coordinate SC dynamics with crossover control, safeguarding meiotic genome transmission.

Indexed as

Cysteine EndopeptidasesNuclear Pore Complex ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSumoylationSynaptonemal ComplexCell Cycle ProteinsCrossing Over, GeneticMeiosisNuclear PoreNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesUbiquitin-Protein LigasesCDC5 protein, S cerevisiaeCell Cycle ProteinsCysteine EndopeptidasesEcm11 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSiz2 protein, S cerevisiaeUbiquitin-Protein LigasesUlp1 proteaseCP: cell biologyCP: molecular biologymeiosisnuclear basketnuclear pore complexrecombinationSUMO proteasesynaptonemal complex central element

Identifiers

PMID42284145
PMCPMC13384433

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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.