Evidence map›Paper›PMID 29980677›Full record

ArticleNature communications2018

Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate.

Daria Trofimova, Mohammadjavad Paydar, Anthony Zara, Lama Talje, Benjamin H Kwok, John S Allingham

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  9. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  10. Review
  11. Article
  12. Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. KIF2A deficiency causes early-onset neurodegeneration.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

6 authors at 3 institutions in 1 country.

Daria TrofimovaDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada.
Mohammadjavad PaydarInstitute for Research in Immunology and Cancer (IRIC), Département de médecine, Université de Montréal, P.O. Box 6128, Station Centre-Ville, Montréal, QC, H3C 3J7, Canada.
Anthony ZaraDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada.
Lama TaljeInstitute for Research in Immunology and Cancer (IRIC), Département de médecine, Université de Montréal, P.O. Box 6128, Station Centre-Ville, Montréal, QC, H3C 3J7, Canada.
Benjamin H KwokInstitute for Research in Immunology and Cancer (IRIC), Département de médecine, Université de Montréal, P.O. Box 6128, Station Centre-Ville, Montréal, QC, H3C 3J7, Canada. benjamin.kwok@umontreal.ca.
John S AllinghamDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada. allinghj@queensu.ca.
Queen's University · CAUniversité de Montréal · CAInstitute for Research in Immunology and Cancer · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin-13 proteins are major microtubule (MT) regulatory factors that catalyze removal of tubulin subunits from MT ends. The class-specific "neck" and loop 2 regions of these motors are required for MT depolymerization, but their contributing roles are still unresolved because their interactions with MT ends have not been observed directly. Here we report the crystal structure of a catalytically active kinesin-13 monomer (Kif2A) in complex with two bent αβ-tubulin heterodimers in a head-to-tail array, providing a view of these interactions. The neck of Kif2A binds to one tubulin dimer and the motor core to the other, guiding insertion of the KVD motif of loop 2 in between them. AMPPNP-bound Kif2A can form stable complexes with tubulin in solution and trigger MT depolymerization. We also demonstrate the importance of the neck in modulating ATP turnover and catalytic depolymerization of MTs. These results provide mechanistic insights into the catalytic cycles of kinesin-13.

Indexed as

PolymerizationProtein MultimerizationAdenosine TriphosphateAmino Acid SequenceAnimalsCattleHumansKinesinsMicrotubulesProtein BindingProtein DomainsProtein Structure, SecondaryRecombinant Fusion ProteinsTubulinAdenosine TriphosphateKIF13A protein, humanKIF2A protein, humanKinesinsRecombinant Fusion ProteinsTubulin

Identifiers

PMID29980677
PMCPMC6035175
OpenAlexW2811082648

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.