Evidence map›Paper›PMID 19116309›Full record

ArticleMolecular biology of the cell2009

Kinesin-14 family proteins HSET/XCTK2 control spindle length by cross-linking and sliding microtubules.

Shang Cai, Lesley N Weaver, Stephanie C Ems-McClung, Claire E Walczak

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

116 citing papers in PubMed, 197 citations in OpenAlex.

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  7. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
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  20. Mechanisms underlying spindle assembly and robustness.Nature reviews. Molecular cell biology · 2023
    Review

56 more citing papers are in PubMed but not listed here.

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.

Shang CaiBiochemistry Program, Indiana University, Bloomington, IN 47405, USA.
Lesley N Weaver
Stephanie C Ems-McClung
Claire E Walczak
Indiana University Bloomington · US

Funding

Mechanisms of Spindle AssemblyR01GM059618 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WALCZAK, CLAIRE E · 1999 to 2016
$4.7M
Acquisition of a High-throughput Confocal Imaging SystemS10RR025033 · NCRR · INDIANA UNIVERSITY INDIANAPOLIS · PI WALCZAK, CLAIRE E · 2008 to 2008
$927k
NCRR NIH HHS S10 RR025033NCRR NIH HHS S10RR025033-01NIGMS NIH HHS GM59618NIGMS NIH HHS R01 GM059618
6 · The paper itself

Abstract

Kinesin-14 family proteins are minus-end directed motors that cross-link microtubules and play key roles during spindle assembly. We showed previously that the Xenopus Kinesin-14 XCTK2 is regulated by Ran via the association of a bipartite NLS in the tail of XCTK2 with importin alpha/beta, which regulates its ability to cross-link microtubules during spindle formation. Here we show that mutation of the nuclear localization signal (NLS) of human Kinesin-14 HSET caused an accumulation of HSET in the cytoplasm, which resulted in strong microtubule bundling. HSET overexpression in HeLa cells resulted in longer spindles, similar to what was seen with NLS mutants of XCTK2 in extracts, suggesting that Kinesin-14 proteins play similar roles in extracts and in somatic cells. Conversely, HSET knockdown by RNAi resulted in shorter spindles but did not affect pole formation. The change in spindle length was not dependent on K-fibers, as elimination of the K-fiber by Nuf2 RNAi resulted in an increase in spindle length that was partially rescued by co-RNAi of HSET. However, these changes in spindle length did require microtubule sliding, as overexpression of an HSET mutant that had its sliding activity uncoupled from its ATPase activity resulted in cells with spindle lengths shorter than cells overexpressing wild-type HSET. Our results are consistent with a model in which Ran regulates the association of Kinesin-14s with importin alpha/beta to prevent aberrant cross-linking and bundling of microtubules by sequestering Kinesin-14s in the nucleus during interphase. Kinesin-14s act during mitosis to cross-link and slide between parallel microtubules to regulate spindle length.

Indexed as

alpha KaryopherinsAnimalsbeta KaryopherinsCytoplasmGreen Fluorescent ProteinsHeLa CellsHumansInterphaseKinesinsMicrotubulesMutationNuclear Localization Signalsran GTP-Binding ProteinRecombinant Fusion ProteinsRNA InterferenceSpindle Apparatusalpha Karyopherinsbeta KaryopherinsGreen Fluorescent ProteinsKIFC1 protein, humanKIFC1 protein, XenopusKinesinsNuclear Localization Signalsran GTP-Binding ProteinRAN protein, humanRecombinant Fusion ProteinsXenopus Proteins

Identifiers

PMID19116309
PMCPMC2649268
OpenAlexW2111406540

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.