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

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

Research output: Contribution to journalArticle

8 Citations (Scopus)

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.

Original languageEnglish (US)
Article number1662
JournalNature Communications
Volume9
Issue number1
DOIs
StatePublished - Dec 1 2018

Fingerprint

depolymerization
Kinesin
Depolymerization
Microtubules
nucleotides
proteins
Drosophila
locomotion
Tubulin
electron microscopy
curvature
Nucleotides
Microtubule Proteins
Cryoelectron Microscopy
Drosophila melanogaster
Electron microscopy
Catalytic Domain

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s. / Benoit, Matthieu P.M.H.; Asenjo, Ana B.; Sosa, Hernando J.

In: Nature Communications, Vol. 9, No. 1, 1662, 01.12.2018.

Research output: Contribution to journalArticle

@article{3ab73680c7014cdc841ca2d5740c79c1,
title = "Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s",
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.",
author = "Benoit, {Matthieu P.M.H.} and Asenjo, {Ana B.} and Sosa, {Hernando J.}",
year = "2018",
month = "12",
day = "1",
doi = "10.1038/s41467-018-04044-8",
language = "English (US)",
volume = "9",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

TY - JOUR

T1 - Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s

AU - Benoit, Matthieu P.M.H.

AU - Asenjo, Ana B.

AU - Sosa, Hernando J.

PY - 2018/12/1

Y1 - 2018/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85046149090&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85046149090&partnerID=8YFLogxK

U2 - 10.1038/s41467-018-04044-8

DO - 10.1038/s41467-018-04044-8

M3 - Article

VL - 9

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 1662

ER -