Evidence map›Paper›PMID 30017484›Full record

ArticleCurrent biology : CB2018

Processive Kinesin-14 HSET Exhibits Directional Flexibility Depending on Motor Traffic.

Dana N Reinemann, Stephen R Norris, Ryoma Ohi, Matthew J Lang

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Single-molecule investigations of single-chain cellulose biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Cross-linker design determines microtubule network organization by opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
  19. Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

4 authors at 2 institutions in 1 country.

Dana N ReinemannDepartment of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN 37235, USA.
Stephen R NorrisDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
Ryoma OhiDepartment of Cell and Developmental Biology and LSI, University of Michigan School of Medicine, Ann Arbor, MI 48109-2216, USA.
Matthew J LangDepartment of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN 37235, USA; Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, TN 37232, USA. Electronic address: matt.lang@vanderbilt.edu.
Vanderbilt University · USUniversity of Michigan · US

Funding

Regulation of microtubule dynamics during cell divisionR01GM086610 · NIGMS · VANDERBILT UNIVERSITY · PI OHI, RYOMA · 2010 to 2023
$4.5M
NIGMS NIH HHS R01 GM086610
6 · The paper itself

Abstract

A common mitotic defect observed in cancer cells that possess supernumerary (more than two) centrosomes is multipolar spindle formation [1, 2]. Such structures are resolved into a bipolar geometry by minus-end-directed motor proteins, such as cytoplasmic dynein and the kinesin-14 HSET [3-8]. HSET is also thought to antagonize plus-end-directed kinesin-5 Eg5 to balance spindle forces [4, 5, 7, 9]. However, the biomechanics of this force opposition are unclear, as HSET has previously been defined as a non-processive motor [10-16]. Here, we use optical trapping to elucidate the mechanism of force generation by HSET. We show that a single HSET motor has a processive nature with the ability to complete multiple steps while trapped along a microtubule and when unloaded can move in both directions for microns. Compared to other kinesins, HSET has a relatively weak stall force of 1.1 pN [17, 18]. Moreover, HSET's tail domain and its interaction with the E-hook of tubulin are necessary for long-range motility. In vitro polarity-marked bundle assays revealed that HSET selectively generates force in anti-parallel bundles on the order of its stall force. When combined with varied ratios of Eg5, HSET adopts Eg5's directionality while acting as an antagonizing force brake, requiring at least a 10-fold higher Eg5 concentration to surpass HSET's sliding force. These results reveal HSET's ability to change roles within the spindle from acting as an adjustable microtubule slider and force regulator to a processive motor that aids in minus end focusing.

Indexed as

CentrosomeDyneinsKinesinsMicrotubulesSpindle ApparatusTubulinDyneinsKinesinsTubulinEg5HSETkinesin-14mitotic spindleoptical trapprocessivitysingle molecule

Identifiers

PMID30017484
PMCPMC11009875
OpenAlexW2884525838

What OpenQuestion holds

Textmetadata
LicenceTDM
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.