Evidence map›Paper›PMID 25940345›Full record

ArticleThe Journal of cell biology2015

Hsp72 is targeted to the mitotic spindle by Nek6 to promote K-fiber assembly and mitotic progression.

Laura O'Regan, Josephina Sampson, Mark W Richards, Axel Knebel, Daniel Roth, Fiona E Hood, Anne Straube, Stephen J Royle, Richard Bayliss, Andrew M Fry

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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 at 3 institutions in 1 country.

Laura O'ReganDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, England, UK.
Josephina SampsonDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, England, UK.
Mark W RichardsDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, England, UK.
Axel KnebelKinasource Ltd, The Sir James Black Center, Dundee DD1 5EH, Scotland, UK.
Daniel RothCentre for Mechanochemical Cell Biology, Warwick Medical School, Coventry CV4 7AL, England, UK.
Fiona E HoodDepartment of Cellular and Molecular Physiology, University of Liverpool, Liverpool L69 3BX, England, UK.
Anne StraubeCentre for Mechanochemical Cell Biology, Warwick Medical School, Coventry CV4 7AL, England, UK.
Stephen J RoyleCentre for Mechanochemical Cell Biology, Warwick Medical School, Coventry CV4 7AL, England, UK Department of Cellular and Molecular Physiology, University of Liverpool, Liverpool L69 3BX, England, UK.
Richard BaylissDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, England, UK.
Andrew M FryDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, England, UK amf5@le.ac.uk.
University of Leicester · GBUniversity of Warwick · GBUniversity of Liverpool · GB

Funding

Cancer Research UK 12772Cancer Research UK 15182Cancer Research UK C1362/A18081Cancer Research UK C24461/A12772Cancer Research UK C25425/A15182Medical Research CouncilWellcome TrustWellcome Trust 082828Wellcome Trust 097828Worldwide Cancer Research 13-0042Worldwide Cancer Research 16-0119
6 · The paper itself

Abstract

Hsp70 proteins represent a family of chaperones that regulate cellular homeostasis and are required for cancer cell survival. However, their function and regulation in mitosis remain unknown. In this paper, we show that the major inducible cytoplasmic Hsp70 isoform, Hsp72, is required for assembly of a robust bipolar spindle capable of efficient chromosome congression. Mechanistically, Hsp72 associates with the K-fiber-stabilizing proteins, ch-TOG and TACC3, and promotes their interaction with each other and recruitment to spindle microtubules (MTs). Targeting of Hsp72 to the mitotic spindle is dependent on phosphorylation at Thr-66 within its nucleotide-binding domain by the Nek6 kinase. Phosphorylated Hsp72 concentrates on spindle poles and sites of MT-kinetochore attachment. A phosphomimetic Hsp72 mutant rescued defects in K-fiber assembly, ch-TOG/TACC3 recruitment and mitotic progression that also resulted from Nek6 depletion. We therefore propose that Nek6 facilitates association of Hsp72 with the mitotic spindle, where it promotes stable K-fiber assembly through recruitment of the ch-TOG-TACC3 complex.

Indexed as

HEK293 CellsHeLa CellsHSP72 Heat-Shock ProteinsHumansKinetochoresMicrotubule-Associated ProteinsMicrotubulesMitosisMutationNIMA-Related KinasesProtein Serine-Threonine KinasesSpindle ApparatusCKAP5 protein, humanHSP72 Heat-Shock ProteinsMicrotubule-Associated ProteinsNEK6 protein, humanNIMA-Related KinasesProtein Serine-Threonine KinasesTACC3 protein, human

Identifiers

PMID25940345
PMCPMC4427782
OpenAlexW2124394520

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.