Evidence map›Paper›PMID 36259662›Full record

ArticleBiology open2022

Phosphosites of the yeast centrosome component Spc110 contribute to cell cycle progression and mitotic exit.

Marjan Abbasi, Alexander Julner, Yan Ting Lim, Tianyun Zhao, Radoslaw Mikolaj Sobota, Victoria Menéndez-Benito

Open access · goldAbstract read
In one paragraph

Article in Biology open, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

2 citing papers in PubMed, 6 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
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 2 institutions in 2 countries.

Marjan AbbasiDepartment of Biosciences and Nutrition, Karolinska Institutet, SE-141 83 Huddinge, Sweden.ORCID 0000-0002-4221-0984
Alexander JulnerDepartment of Biosciences and Nutrition, Karolinska Institutet, SE-141 83 Huddinge, Sweden.ORCID 0000-0001-7605-5313
Yan Ting LimFunctional Proteomics Laboratory, SingMass National Laboratory, Institute for Molecular and Cell Biology (IMCB), Agency for Science, Technology, and Research (A*Star), 138 673 Proteos, Singapore.ORCID 0000-0003-2886-126X
Tianyun ZhaoFunctional Proteomics Laboratory, SingMass National Laboratory, Institute for Molecular and Cell Biology (IMCB), Agency for Science, Technology, and Research (A*Star), 138 673 Proteos, Singapore.ORCID 0000-0002-2035-6026
Radoslaw Mikolaj SobotaFunctional Proteomics Laboratory, SingMass National Laboratory, Institute for Molecular and Cell Biology (IMCB), Agency for Science, Technology, and Research (A*Star), 138 673 Proteos, Singapore.ORCID 0000-0002-2455-2526
Victoria Menéndez-BenitoDepartment of Biosciences and Nutrition, Karolinska Institutet, SE-141 83 Huddinge, Sweden.
Agency for Science, Technology and Research · SGKarolinska Institutet · SE

Funding

Carl Tryggers Stiftelse fur Vetenskaplig Forskning CTS 16:311Karolinska InstitutetSingapore National Research FoundationVetenskapsrådet (The Swedish Research Council) VR-NT 2013-04491Vetenskapsrdet 2013-04491
6 · The paper itself

Abstract

Spc110 is an essential component of the spindle pole body (SPB), the yeast equivalent of the centrosome, that recruits the γ-tubulin complex to the nuclear side of the SPB to produce the microtubules that form the mitotic spindle. Here, we identified phosphosites S11 and S36 in maternally originated Spc110 and explored their functions in vivo. Yeast expressing non-phosphorylatable Spc110S11A had a distinct spindle phenotype characterised by higher levels of α-tubulin, which was frequently asymmetrically distributed between the two SPBs. Furthermore, expression of the double mutant Spc110S11AS36A had a delayed cell cycle progression. Specifically, the final steps of mitosis were delayed in Spc110S11AS36A cells, including expression and degradation of the mitotic cyclin Clb2, disassembling the mitotic spindle and re-localizing Cdc14 to the nucleoli, resulting in late mitotic exit and entry in G1. Thus, we propose that Spc110 phosphorylation at S11 and S36 is required to regulate timely cell cycle progression in budding yeast. This article has an associated First Person interview with the first author of the paper.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCalmodulin-Binding ProteinsCell Cycle ProteinsCentrosomeCytoskeletal ProteinsMitosisProtein Tyrosine PhosphatasesSpindle ApparatusSpindle Pole BodiesCalmodulin-Binding ProteinsCDC14 protein, S cerevisiaeCell Cycle ProteinsCytoskeletal ProteinsProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsSPC110 protein, S cerevisiaeCdc14MicrotubuleMitotic spindlePericentrinPhosphorylationSpindle pole body

Identifiers

PMID36259662
PMCPMC9672857
OpenAlexW4306790043

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.