Evidence map›Paper›PMID 26906737›Full record

ArticleDevelopmental cell2016

Regulation of a Spindle Positioning Factor at Kinetochores by SUMO-Targeted Ubiquitin Ligases.

Jörg Schweiggert, Lea Stevermann, Davide Panigada, Daniel Kammerer, Dimitris Liakopoulos

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Developmental cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-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

18 citing papers in PubMed, 27 citations in OpenAlex.

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  14. Nuclear movement in fungi.Seminars in cell & developmental biology · 2018
    Review
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  17. Go in! Go out! Inducible control of nuclear localization.Current opinion in chemical biology · 2016
    Review
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Jörg SchweiggertCentre de Recherche de Biochimie Macromoléculaire (CRBM), CNRS UMR 5237, 1919 route de Mende, 34293 Montpellier Cedex 05, France; Biochemistry Centre Heidelberg (BZH), INF 328, 69120 Heidelberg, Germany; The Hartmut Hoffmann-Berling International Graduate School of Molecular and Cellular Biology, University of Heidelberg, 69117 Heidelberg, Germany.
Lea StevermannBiochemistry Centre Heidelberg (BZH), INF 328, 69120 Heidelberg, Germany; The Hartmut Hoffmann-Berling International Graduate School of Molecular and Cellular Biology, University of Heidelberg, 69117 Heidelberg, Germany.
Davide PanigadaCentre de Recherche de Biochimie Macromoléculaire (CRBM), CNRS UMR 5237, 1919 route de Mende, 34293 Montpellier Cedex 05, France.
Daniel KammererBiochemistry Centre Heidelberg (BZH), INF 328, 69120 Heidelberg, Germany.
Dimitris LiakopoulosCentre de Recherche de Biochimie Macromoléculaire (CRBM), CNRS UMR 5237, 1919 route de Mende, 34293 Montpellier Cedex 05, France; Biochemistry Centre Heidelberg (BZH), INF 328, 69120 Heidelberg, Germany; The Hartmut Hoffmann-Berling International Graduate School of Molecular and Cellular Biology, University of Heidelberg, 69117 Heidelberg, Germany. Electronic address: dimitris.liakopoulos@crbm.cnrs.fr.
Centre National de la Recherche Scientifique · FRHeidelberg Engineering (Germany) · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Correct function of the mitotic spindle requires balanced interplay of kinetochore and astral microtubules that mediate chromosome segregation and spindle positioning, respectively. Errors therein can cause severe defects ranging from aneuploidy to developmental disorders. Here, we describe a protein degradation pathway that functionally links astral microtubules to kinetochores via regulation of a microtubule-associated factor. We show that the yeast spindle positioning protein Kar9 localizes not only to astral but also to kinetochore microtubules, where it becomes targeted for proteasomal degradation by the SUMO-targeted ubiquitin ligases (STUbLs) Slx5-Slx8. Intriguingly, this process does not depend on preceding sumoylation of Kar9 but rather requires SUMO-dependent recruitment of STUbLs to kinetochores. Failure to degrade Kar9 leads to defects in both chromosome segregation and spindle positioning. We propose that kinetochores serve as platforms to recruit STUbLs in a SUMO-dependent manner in order to ensure correct spindle function by regulating levels of microtubule-associated proteins.

Indexed as

Chromosome SegregationKinetochoresMicrotubule-Associated ProteinsMicrotubulesNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsSpindle ApparatusUbiquitin-Protein LigasesKAR9 protein, S cerevisiaeMicrotubule-Associated ProteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Protein Ligases

Identifiers

PMID26906737
OpenAlexW2275585333

What OpenQuestion holds

Textmetadata
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.