Evidence map›Paper›PMID 28232523›Full record

ArticleJournal of cell science2017

GSK3-mediated CLASP2 phosphorylation modulates kinetochore dynamics.

Hayley Pemble, Praveen Kumar, Jeffrey van Haren, Torsten Wittmann

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

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  5. Evidence for coopetition at the maternal-fetal interface shaping placental invasion.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

4 authors at 1 institution in 1 country.

Hayley PembleDepartment of Cell & Tissue Biology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143, USA.
Praveen KumarDepartment of Cell & Tissue Biology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143, USA.
Jeffrey van HarenDepartment of Cell & Tissue Biology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143, USA.
Torsten WittmannDepartment of Cell & Tissue Biology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143, USA torsten.wittmann@ucsf.edu.ORCID 0000-0001-9134-691X
University of California, San Francisco · US

Funding

Microtubule dynamics during cell polarity and migrationR01GM079139 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WITTMANN, TORSTEN · 2008 to 2017
$2.7M
Spinning disk confocal / FRAP microscope for quantitative live cell imagingS10RR026758 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WITTMANN, TORSTEN · 2010 to 2010
$500k
NCRR NIH HHS S10 RR026758NIGMS NIH HHS R01 GM079139
6 · The paper itself

Abstract

Error-free chromosome segregation requires dynamic control of microtubule attachment to kinetochores, but how kinetochore-microtubule interactions are spatially and temporally controlled during mitosis remains incompletely understood. In addition to the NDC80 microtubule-binding complex, other proteins with demonstrated microtubule-binding activities localize to kinetochores. One such protein is the cytoplasmic linker-associated protein 2 (CLASP2). Here, we show that global GSK3-mediated phosphorylation of the longest isoform, CLASP2α, largely abolishes CLASP2α-microtubule association in metaphase. However, it does not directly control localization of CLASP2α to kinetochores. Using dominant phosphorylation-site variants, we find that CLASP2α phosphorylation weakens kinetochore-microtubule interactions as evidenced by decreased tension between sister kinetochores. Expression of CLASP2α phosphorylation-site mutants also resulted in increased chromosome segregation defects, indicating that GSK3-mediated control of CLASP2α-microtubule interactions contributes to correct chromosome dynamics. Because of global inhibition of CLASP2α-microtubule interactions, we propose a model in which only kinetochore-bound CLASP2α is dephosphorylated, locally engaging its microtubule-binding activity.

Indexed as

CDC2 Protein KinaseCell LineChromosome SegregationCyclin-Dependent KinasesCytoskeletal ProteinsGlycogen Synthase Kinase 3HumansKeratinocytesKinetochoresMicrotubule-Associated ProteinsMicrotubulesMitosisMutationNuclear ProteinsPhosphorylationProtein BindingCDC2 Protein KinaseCDK1 protein, humanCLASP2 protein, humanCyclin-Dependent KinasesCytoskeletal ProteinsGlycogen Synthase Kinase 3Microtubule-Associated ProteinsNDC80 protein, humanNuclear ProteinsCLASP2GSK3KinetochoreMicrotubuleMitosisPhosphorylation

Identifiers

PMID28232523
PMCPMC5399784
OpenAlexW2589938762

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.