Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape

Byron Hunter; Matthieu P. M. H. Benoit; Ana B. Asenjo; Caitlin Doubleday; Daria Trofimova; Corey Frazer; Irsa Shoukat; Hernando Sosa; John S. Allingham

doi:10.1038/s41467-022-31794-3

Nature Communications (Jul 2022)

Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape

Byron Hunter,
Matthieu P. M. H. Benoit,
Ana B. Asenjo,
Caitlin Doubleday,
Daria Trofimova,
Corey Frazer,
Irsa Shoukat,
Hernando Sosa,
John S. Allingham

Affiliations

Byron Hunter: Department of Biomedical and Molecular Sciences, Queen’s University
Matthieu P. M. H. Benoit: Department of Biochemistry, Albert Einstein College of Medicine
Ana B. Asenjo: Department of Biochemistry, Albert Einstein College of Medicine
Caitlin Doubleday: Department of Biomedical and Molecular Sciences, Queen’s University
Daria Trofimova: Department of Biomedical and Molecular Sciences, Queen’s University
Corey Frazer: Department of Molecular Microbiology and Immunology, Brown University
Irsa Shoukat: Department of Biomedical and Molecular Sciences, Queen’s University
Hernando Sosa: Department of Biochemistry, Albert Einstein College of Medicine
John S. Allingham: Department of Biomedical and Molecular Sciences, Queen’s University

DOI: https://doi.org/10.1038/s41467-022-31794-3
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 19

Abstract

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Kinesin-8s are dual-activity motor proteins that can move processively on microtubules and depolymerize microtubule plus-ends. This study shows how kinesin-8s alternate between a promotility and a pro-microtubule-depolymerization state via their tubulin shape-sensing loop-2 region.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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