Evidence map›Paper›PMID 28290984›Full record

ArticleeLife2017

Kinesin-4 KIF21B is a potent microtubule pausing factor.

Wilhelmina E van Riel, Ankit Rai, Sarah Bianchi, Eugene A Katrukha, Qingyang Liu, Albert Jr Heck, Casper C Hoogenraad, Michel O Steinmetz, Lukas C Kapitein, Anna Akhmanova

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 66 citations in OpenAlex.

  1. Microtubule Engagement by the WD40-Containing Tail of Kinesin-4 KIF21B.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. TUBB3 and KIF21A in neurodevelopment and disease.Frontiers in neuroscience · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  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 2 institutions in 2 countries.

Wilhelmina E van RielCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.
Ankit RaiCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.ORCID 0000-0002-1569-0919
Sarah BianchiLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, Switzerland.
Eugene A KatrukhaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.
Qingyang LiuCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.
Albert Jr HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences and The Netherlands Proteomics Centre, Utrecht University, Utrecht, Netherlands.ORCID 0000-0002-2405-4404
Casper C HoogenraadCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.
Michel O SteinmetzLaboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, Switzerland.
Lukas C KapiteinCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.ORCID 0000-0001-9418-6739
Anna AkhmanovaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands.ORCID 0000-0002-9048-8614
Utrecht University · NLPaul Scherrer Institute · CH

Funding

European Research Council 609822
6 · The paper itself

Abstract

Microtubules are dynamic polymers that in cells can grow, shrink or pause, but the factors that promote pausing are poorly understood. Here, we show that the mammalian kinesin-4 KIF21B is a processive motor that can accumulate at microtubule plus ends and induce pausing. A few KIF21B molecules are sufficient to induce strong growth inhibition of a microtubule plus end in vitro. This property depends on non-motor microtubule-binding domains located in the stalk region and the C-terminal WD40 domain. The WD40-containing KIF21B tail displays preference for a GTP-type over a GDP-type microtubule lattice and contributes to the interaction of KIF21B with microtubule plus ends. KIF21B also contains a motor-inhibiting domain that does not fully block the interaction of the protein with microtubules, but rather enhances its pause-inducing activity by preventing KIF21B detachment from microtubule tips. Thus, KIF21B combines microtubule-binding and regulatory activities that together constitute an autonomous microtubule pausing factor.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsHEK293 CellsHumansKinesinsMicrotubulesProtein BindingProtein DomainsProtein Interaction MappingProtein MultimerizationKIF21B protein, humanKinesinsbiophysicscell biologyEB1humanKIF21BKinesinKinesin-4microtubule dynamicspausingstructural biology

Identifiers

PMID28290984
PMCPMC5383399
OpenAlexW2604580983

What OpenQuestion holds

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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.