Evidence map›Paper›PMID 22363481›Full record

ArticlePloS one2012

S. pombe kinesins-8 promote both nucleation and catastrophe of microtubules.

Muriel Erent, Douglas R Drummond, Robert A Cross

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
2.7field-weighted citation impact, top 10% 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, 51 citations in OpenAlex.

  1. Article
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  7. Review
  8. Bioenergetics of theBiomolecules · 2020
    Article
  9. Article
  10. The Journal of cell biology · 2019
    Article
  11. Review
  12. Article
  13. Structural basis of human kinesin-8 function and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

3 authors at 1 institution in 1 country.

Muriel ErentCentre for Mechanochemical Cell Biology, Warwick Medical School, The University of Warwick, Coventry, United Kingdom.
Douglas R Drummond
Robert A Cross
University of Warwick · GB

Funding

Medical Research Council G0200542
6 · The paper itself

Abstract

The kinesins-8 were originally thought to be microtubule depolymerases, but are now emerging as more versatile catalysts of microtubule dynamics. We show here that S. pombe Klp5-436 and Klp6-440 are non-processive plus-end-directed motors whose in vitro velocities on S. pombe microtubules at 7 and 23 nm s(-1) are too slow to keep pace with the growing tips of dynamic interphase microtubules in living S. pombe. In vitro, Klp5 and 6 dimers exhibit a hitherto-undescribed combination of strong enhancement of microtubule nucleation with no effect on growth rate or catastrophe frequency. By contrast in vivo, both Klp5 and Klp6 promote microtubule catastrophe at cell ends whilst Klp6 also increases the number of interphase microtubule arrays (IMAs). Our data support a model in which Klp5/6 bind tightly to free tubulin heterodimers, strongly promoting the nucleation of new microtubules, and then continue to land as a tubulin-motor complex on the tips of growing microtubules, with the motors then dissociating after a few seconds residence on the lattice. In vivo, we predict that only at cell ends, when growing microtubule tips become lodged and their growth slows down, will Klp5/6 motor activity succeed in tracking growing microtubule tips. This mechanism would allow Klp5/6 to detect the arrival of microtubule tips at cells ends and to amplify the intrinsic tendency for microtubules to catastrophise in compression at cell ends. Our evidence identifies Klp5 and 6 as spatial regulators of microtubule dynamics that enhance both microtubule nucleation at the cell centre and microtubule catastrophe at the cell ends.

Indexed as

Adenosine TriphosphatasesAnimalsEnzyme-Linked Immunosorbent AssayGene DeletionGuanosine TriphosphateKinesinsMicrospheresMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalMultiprotein ComplexesProtein MultimerizationProtein StabilityProtein TransportSchizosaccharomycesSchizosaccharomyces pombe Proteins5'-guanylylmethylenebisphosphonateAdenosine TriphosphatasesGuanosine TriphosphateKinesinsKlp5 protein, S pombeKlp6 protein, S pombeMicrotubule-Associated ProteinsMultiprotein ComplexesSchizosaccharomyces pombe ProteinsTubulin

Identifiers

PMID22363481
PMCPMC3282699
OpenAlexW2084631526

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.