Evidence map›Paper›PMID 21378308›Full record

ArticleJournal of cell science2011

Phospho-regulation of kinesin-5 during anaphase spindle elongation.

Rachel Avunie-Masala, Natalia Movshovich, Yael Nissenkorn, Adina Gerson-Gurwitz, Vladimir Fridman, Mardo Kõivomägi, Mart Loog, M Andrew Hoyt, Arieh Zaritsky, Larisa Gheber

Abstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

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  10. Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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.

Rachel Avunie-MasalaDepartment of Clinical Biochemistry, Ben-Gurion University of the Negev, PO Box 653, Beer-Sheva, 84105, Israel.
Natalia Movshovich
Yael Nissenkorn
Adina Gerson-Gurwitz
Vladimir Fridman
Mardo Kõivomägi
Mart Loog
M Andrew Hoyt
Arieh Zaritsky
Larisa Gheber

Funding

Wellcome TrustWellcome Trust 079014/Z/06/Z
6 · The paper itself

Abstract

The kinesin-5 Saccharomyces cerevisiae homologue Cin8 is shown here to be differentially phosphorylated during late anaphase at Cdk1-specific sites located in its motor domain. Wild-type Cin8 binds to the early-anaphase spindles and detaches from the spindles at late anaphase, whereas the phosphorylation-deficient Cin8-3A mutant protein remains attached to a larger region of the spindle and spindle poles for prolonged periods. This localization of Cin8-3A causes faster spindle elongation and longer anaphase spindles, which have aberrant morphology. By contrast, the phospho-mimic Cin8-3D mutant exhibits reduced binding to the spindles. In the absence of the kinesin-5 homologue Kip1, cells expressing Cin8-3D exhibit spindle assembly defects and are not viable at 37°C as a result of spindle collapse. We propose that dephosphorylation of Cin8 promotes its binding to the spindle microtubules before the onset of anaphase. In mid to late anaphase, phosphorylation of Cin8 causes its detachment from the spindles, which reduces the spindle elongation rate and aids in maintaining spindle morphology.

Indexed as

AnaphaseCDC2 Protein KinaseKinesinsMicrotubulesPhosphorylationProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusCDC2 Protein KinaseCIN8 protein, S cerevisiaeKinesinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21378308
PMCPMC3048887

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Registered trials

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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.