Evidence map›Paper›PMID 29695795›Full record

ArticleNature communications2018

Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.

Matthieu P M H Benoit, Ana B Asenjo, Hernando Sosa

Erratum issuedOpen 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. An erratum has been issued. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
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  7. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  8. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
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  11. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Matthieu P M H BenoitDepartment of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA.
Ana B AsenjoDepartment of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA.
Hernando SosaDepartment of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. hernando.sosa@einstein.yu.edu.
Albert Einstein College of Medicine · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
MECHANISM OF MICROTUBULE DYNAMICS REGULATION BY KINESINSR01GM113164 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI HERNANDO Jose SOSA · 2015 to 2026
$5.6M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM113164NIH HHS S10 OD019994
6 · The paper itself

Abstract

Kinesin-13s constitute a distinct group within the kinesin superfamily of motor proteins that promote microtubule depolymerization and lack motile activity. The molecular mechanism by which kinesin-13s depolymerize microtubules and are adapted to perform a seemingly very different activity from other kinesins is still unclear. To address this issue, here we report the near atomic resolution cryo-electron microscopy (cryo-EM) structures of Drosophila melanogaster kinesin-13 KLP10A protein constructs bound to curved or straight tubulin in different nucleotide states. These structures show how nucleotide induced conformational changes near the catalytic site are coupled with movement of the kinesin-13-specific loop-2 to induce tubulin curvature leading to microtubule depolymerization. The data highlight a modular structure that allows similar kinesin core motor-domains to be used for different functions, such as motility or microtubule depolymerization.

Indexed as

Adenosine TriphosphateCell MovementCryoelectron MicroscopyDrosophila ProteinsKinesinsMicrotubulesMolecular Docking SimulationPolymerizationProtein BindingProtein Structure, TertiaryRecombinant ProteinsTubulinAdenosine TriphosphateDrosophila ProteinsKinesinsKLP10A protein, DrosophilaRecombinant ProteinsTubulin

Identifiers

PMID29695795
PMCPMC5916938
OpenAlexW2766903323

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.