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

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  • Matthieu P.M.H. Benoit

    (Albert Einstein College of Medicine)

  • Ana B. Asenjo

    (Albert Einstein College of Medicine)

  • Hernando Sosa

    (Albert Einstein College of Medicine)

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.

Suggested Citation

  • Matthieu P.M.H. Benoit & Ana B. Asenjo & Hernando Sosa, 2018. "Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04044-8
    DOI: 10.1038/s41467-018-04044-8
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    Cited by:

    1. Chunting Zhang & Changmiao Guo & Ryan W. Russell & Caitlin M. Quinn & Mingyue Li & John C. Williams & Angela M. Gronenborn & Tatyana Polenova, 2022. "Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Charles Bayly-Jones & Christopher J. Lupton & Claudia Fritz & Hariprasad Venugopal & Daniel Ramsbeck & Michael Wermann & Christian Jäger & Alex Marco & Stephan Schilling & Dagmar Schlenzig & James C. , 2022. "Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Byron Hunter & Matthieu P. M. H. Benoit & Ana B. Asenjo & Caitlin Doubleday & Daria Trofimova & Corey Frazer & Irsa Shoukat & Hernando Sosa & John S. Allingham, 2022. "Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    4. Tianyang Liu & Fiona Shilliday & Alexander D. Cook & Mohammad Zeeshan & Declan Brady & Rita Tewari & Colin J. Sutherland & Anthony J. Roberts & Carolyn A. Moores, 2022. "Mechanochemical tuning of a kinesin motor essential for malaria parasite transmission," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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