Evidence map›Paper›PMID 37970674›Full record

ArticleJournal of cell science2023

SUMOylation regulates Lem2 function in centromere clustering and silencing.

Joanna Strachan, Orsolya Leidecker, Christos Spanos, Clementine Le Coz, Elliott Chapman, Ana Arsenijevic, Haidao Zhang, Ning Zhao, Steven H Spoel, Elizabeth H Bayne

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

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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 at 3 institutions in 2 countries.

Joanna StrachanInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.
Orsolya LeideckerMax Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
Christos SpanosWellcome Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.ORCID 0000-0002-4376-8242
Clementine Le CozInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.
Elliott ChapmanInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.ORCID 0000-0003-1458-3916
Ana ArsenijevicInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.ORCID 0000-0001-8835-1750
Haidao ZhangInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.
Ning ZhaoInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.
Steven H SpoelInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.ORCID 0000-0003-4340-7591
Elizabeth H BayneInstitute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3FF, UK.ORCID 0000-0001-8775-999X
University of Edinburgh · GBMax Planck Institute for Biology of Ageing · DEWellcome Centre for Cell Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S016767/1Medical Research Council G1000505Wellcome TrustWellcome Trust 202771/Z/16/Z
6 · The paper itself

Abstract

Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here, we show that in the fission yeast Schizosaccharomyces pombe, delocalisation of the SUMO protease Ulp1 from the nuclear envelope results in centromeric defects that can be attributed to hyper-SUMOylation at the nuclear periphery. Unexpectedly, we find that although this localised hyper-SUMOylation impairs centromeric silencing, it can also enhance centromere clustering. Moreover, both effects are at least partially dependent on SUMOylation of the inner nuclear membrane protein Lem2. Lem2 has previously been implicated in diverse biological processes, including the promotion of both centromere clustering and silencing, but how these distinct activities are coordinated was unclear; our observations suggest a model whereby SUMOylation serves as a regulatory switch, modulating Lem2 interactions with competing partner proteins to balance its roles in alternative pathways. Our findings also reveal a previously unappreciated role for SUMOylation in promoting centromere clustering.

Indexed as

SchizosaccharomycesSchizosaccharomyces pombe ProteinsCentromereCluster AnalysisMembrane ProteinsNuclear ProteinsSumoylationMembrane ProteinsNuclear ProteinsSchizosaccharomyces pombe ProteinsCentromeresLem2Schizosaccharomyces pombeSUMOylationUbiquitylation

Identifiers

PMID37970674
PMCPMC10730020
OpenAlexW4388724195

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.