Evidence map›Paper›PMID 28455557›Full record

ArticleCellular and molecular life sciences : CMLS2017

Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase.

Alina Goldstein, Nurit Siegler, Darya Goldman, Haim Judah, Ervin Valk, Mardo Kõivomägi, Mart Loog, Larisa Gheber

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

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0cells of the map it votes in
14citing 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

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3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

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  12. Synthetic-Evolution Reveals Narrow Paths to Regulation of theInternational journal of biological sciences · 2019
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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

8 authors.

Alina GoldsteinDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
Nurit SieglerDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
Darya GoldmanDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
Haim JudahDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
Ervin ValkInstitute of Technology, University of Tartu, Tartu, Estonia.
Mardo KõivomägiInstitute of Technology, University of Tartu, Tartu, Estonia.
Mart LoogInstitute of Technology, University of Tartu, Tartu, Estonia.
Larisa GheberDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel. lgheber@bgu.ac.il.ORCID 0000-0003-3759-4001

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bipolar kinesin-5 motors perform essential functions in mitotic spindle dynamics. We previously demonstrated that phosphorylation of at least one of the Cdk1 sites in the catalytic domain of the Saccharomyces cerevisiae kinesin-5 Cin8 (S277, T285, S493) regulates its localization to the anaphase spindle. The contribution of these three sites to phospho-regulation of Cin8, as well as the timing of such contributions, remains unknown. Here, we examined the function and spindle localization of phospho-deficient (serine/threonine to alanine) and phospho-mimic (serine/threonine to aspartic acid) Cin8 mutants. In vitro, the three Cdk1 sites undergo phosphorylation by Clb2-Cdk1. In cells, phosphorylation of Cin8 affects two aspects of its localization to the anaphase spindle, translocation from the spindle-pole bodies (SPBs) region to spindle microtubules (MTs) and the midzone, and detachment from the mitotic spindle. We found that phosphorylation of S277 is essential for the translocation of Cin8 from SPBs to spindle MTs and the subsequent detachment from the spindle. Phosphorylation of T285 mainly affects the detachment of Cin8 from spindle MTs during anaphase, while phosphorylation at S493 affects both the translocation of Cin8 from SPBs to the spindle and detachment from the spindle. Only S493 phosphorylation affected the anaphase spindle elongation rate. We conclude that each phosphorylation site plays a unique role in regulating Cin8 functions and postulate a model in which the timing and extent of phosphorylation of the three sites orchestrates the anaphase function of Cin8.

Indexed as

AnaphaseCatalytic DomainCDC2 Protein KinaseCyclin BKinesinsMicrotubulesMutagenesis, Site-DirectedPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusCDC2 Protein KinaseCLB2 protein, S cerevisiaeCyclin BKinesinsSaccharomyces cerevisiae ProteinsAnaphase BCin8Kinesin-5MicrotubulesMitosisPhospho-regulation

Identifiers

PMID28455557
PMCPMC11107736

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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.