Evidence map›Paper›PMID 25875822›Full record

ArticlePLoS biology2015

CYK4 promotes antiparallel microtubule bundling by optimizing MKLP1 neck conformation.

Tim Davies, Noriyuki Kodera, Gabriele S Kaminski Schierle, Eric Rees, Miklos Erdelyi, Clemens F Kaminski, Toshio Ando, Masanori Mishima

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.5field-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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Mechanistic insights into central spindle assembly mediated by the centralspindlin complex.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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 at 3 institutions in 2 countries.

Tim DaviesGurdon Institute, University of Cambridge, Tennis Court Road, Cambridge, United Kingdom.
Noriyuki KoderaDepartment of Physics and Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa, Japan.
Gabriele S Kaminski SchierleDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Pembroke Street, Cambridge, United Kingdom.
Eric ReesDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Pembroke Street, Cambridge, United Kingdom.
Miklos ErdelyiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Pembroke Street, Cambridge, United Kingdom.
Clemens F KaminskiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Pembroke Street, Cambridge, United Kingdom.
Toshio AndoDepartment of Physics and Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa, Japan.
Masanori MishimaBiomedical Cell Biology, Warwick Medical School, University of Warwick, Gibbet Hill Road, Coventry, United Kingdom.
University of Cambridge · GBKanazawa University · JPUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UK 11985Cancer Research UK A11985Cancer Research UK C19769/A6356Cancer Research UK C19769/A7164Medical Research Council MR/K015850/1Wellcome TrustWellcome Trust 089703/Z/09/Z
6 · The paper itself

Abstract

Centralspindlin, a constitutive 2:2 heterotetramer of MKLP1 (a kinesin-6) and the non-motor subunit CYK4, plays important roles in cytokinesis. It is crucial for the formation of central spindle microtubule bundle structure. Its accumulation at the central antiparallel overlap zone is key for recruitment and regulation of downstream cytokinesis factors and for stable anchoring of the plasma membrane at the midbody. Both MKLP1 and CYK4 are required for efficient microtubule bundling. However, the mechanism by which CYK4 contributes to this is unclear. Here we performed structural and functional analyses of centralspindlin using high-speed atomic force microscopy, Fӧrster resonance energy transfer analysis, and in vitro reconstitution. Our data reveal that CYK4 binds to a globular mass in the atypically long MKLP1 neck domain between the catalytic core and the coiled coil and thereby reconfigures the two motor domains in the MKLP1 dimer to be suitable for antiparallel microtubule bundling. Our work provides insights into the microtubule bundling during cytokinesis and into the working mechanisms of the kinesins with non-canonical neck structures.

Indexed as

AnimalsBinding SitesFluorescence Resonance Energy TransferHumansMicroscopy, Atomic ForceMicrotubule-Associated ProteinsMicrotubulesKIF23 protein, humanMicrotubule-Associated Proteins

Identifiers

PMID25875822
PMCPMC4395295
OpenAlexW2150022972

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.