Evidence map›Paper›PMID 34586062›Full record

ArticleeLife2021

Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes nuclear envelope localization during meiosis.

Hanumanthu Bd Prasada Rao, Takeshi Sato, Kiran Challa, Yurika Fujita, Miki Shinohara, Akira Shinohara

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. 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
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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Yeast centrosomes act as organizing centers to promote Polo kinase-mediated adaptation to persistent DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Cyclins and CDKs in the regulation of meiosis-specific events.Frontiers in cell and developmental biology · 2022
    Review
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

6 authors at 4 institutions in 3 countries.

Hanumanthu Bd Prasada RaoInstitute for Protein Research, Osaka University, Suita, Japan.
Takeshi SatoKyoto Pharmaceutical University, Kyoto, Japan.
Kiran ChallaInstitute for Protein Research, Osaka University, Suita, Japan.
Yurika FujitaInstitute for Protein Research, Osaka University, Suita, Japan.
Miki ShinoharaInstitute for Protein Research, Osaka University, Suita, Japan.
Akira ShinoharaInstitute for Protein Research, Osaka University, Suita, Japan.ORCID 0000-0003-4207-8247
Protein Research Foundation · JPKyoto Pharmaceutical University · JPNational Institute of Animal Biotechnology · INPaul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During meiosis, protein ensembles in the nuclear envelope (NE) containing SUN- and KASH-domain proteins, called linker nucleocytoskeleton and cytoskeleton (LINC) complex, promote the chromosome motion. Yeast SUN-domain protein, Mps3, forms multiple meiosis-specific ensembles on NE, which show dynamic localisation for chromosome motion; however, the mechanism by which these Mps3 ensembles are formed during meiosis remains largely unknown. Here, we showed that the cyclin-dependent protein kinase (CDK) and Dbf4-dependent Cdc7 protein kinase (DDK) regulate meiosis-specific dynamics of Mps3 on NE, particularly by mediating the resolution of Mps3 clusters and telomere clustering. We also found that the luminal region of Mps3 juxtaposed to the inner nuclear membrane is required for meiosis-specific localisation of Mps3 on NE. Negative charges introduced by meiosis-specific phosphorylation in the luminal region of Mps3 alter its interaction with negatively charged lipids by electric repulsion in reconstituted liposomes. Phospho-mimetic substitution in the luminal region suppresses the localisation of Mps3 via the inactivation of CDK or DDK. Our study revealed multi-layered phosphorylation-dependent regulation of the localisation of Mps3 on NE for meiotic chromosome motion and NE remodelling.

Indexed as

MeiosisCell Cycle ProteinsCyclin-Dependent KinasesMembrane ProteinsNuclear EnvelopeNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCDC7 protein, S cerevisiaeCell Cycle ProteinsCyclin-Dependent KinasesMembrane ProteinsMps3 protein, S cerevisiaeNuclear ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteinschromosome motionchromosomesgene expressionmeiosisMps3nuclear envelopephosphorylationS. cerevisiaesun domain

Identifiers

PMID34586062
PMCPMC8570693
OpenAlexW3202706086

What OpenQuestion holds

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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.