Evidence map›Paper›PMID 29397398›Full record

ReviewCellular and molecular life sciences : CMLS2018

Bidirectional motility of kinesin-5 motor proteins: structural determinants, cumulative functions and physiological roles.

Sudhir Kumar Singh, Himanshu Pandey, Jawdat Al-Bassam, Larisa Gheber

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 58 citations in OpenAlex.

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  9. 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

4 authors at 2 institutions in 2 countries.

Sudhir Kumar SinghDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
Himanshu PandeyDepartment of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
Jawdat Al-BassamDepartment of Molecular and Cellular Biology, University of California, Davis, Davis, CA, 95616, USA.
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
Ben-Gurion University of the Negev · ILUniversity of California, Davis · US

Funding

Israel Science Foundation 165/13National Science Foundation NSF-1615991NIH HHS NIH-R01-GM11283United States-Israel Binational Science Foundation BSF-2015851
6 · The paper itself

Abstract

Mitotic kinesin-5 bipolar motor proteins perform essential functions in mitotic spindle dynamics by crosslinking and sliding antiparallel microtubules (MTs) apart within the mitotic spindle. Two recent studies have indicated that single molecules of Cin8, the Saccharomyces cerevisiae kinesin-5 homolog, are minus end-directed when moving on single MTs, yet switch directionality under certain experimental conditions (Gerson-Gurwitz et al., EMBO J 30:4942-4954, 2011; Roostalu et al., Science 332:94-99, 2011). This finding was unexpected since the Cin8 catalytic motor domain is located at the N-terminus of the protein, and such kinesins have been previously thought to be exclusively plus end-directed. In addition, the essential intracellular functions of kinesin-5 motors in separating spindle poles during mitosis can only be accomplished by plus end-directed motility during antiparallel sliding of the spindle MTs. Thus, the mechanism and possible physiological role of the minus end-directed motility of kinesin-5 motors remain unclear. Experimental and theoretical studies from several laboratories in recent years have identified additional kinesin-5 motors that are bidirectional, revealed structural determinants that regulate directionality, examined the possible mechanisms involved and have proposed physiological roles for the minus end-directed motility of kinesin-5 motors. Here, we summarize our current understanding of the remarkable ability of certain kinesin-5 motors to switch directionality when moving along MTs.

Indexed as

AnimalsHumansKinesinsMolecular Motor ProteinsMovementProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCIN8 protein, S cerevisiaeKinesinsMolecular Motor ProteinsSaccharomyces cerevisiae ProteinsBidirectionalityControl of kinesin motilityIn-vitro motility assaysKinesin-5MicrotubulesMitosis

Identifiers

PMID29397398
PMCPMC11105280
OpenAlexW2785432690

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.