Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding

Marcus Braun, Zdenek Lansky, Agata Szuba, Friedrich W. Schwarz, Aniruddha Mitra, Mengfei Gao, Annemarie Lüdecke, Pieter Rein Ten Wolde, Stefan Diez

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Microtubule-crosslinking motor proteins, which slide antiparallel microtubules, are required for the remodeling of microtubule networks. Hitherto, all microtubule-crosslinking motors have been shown to slide microtubules at a constant velocity until no overlap remains between them, leading to the breakdown of the initial microtubule geometry. Here, we show in vitro that the sliding velocity of microtubules, driven by human kinesin-14 HSET, decreases when microtubules start to slide apart, resulting in the maintenance of finite-length microtubule overlaps. We quantitatively explain this feedback using the local interaction kinetics of HSET with overlapping microtubules that cause retention of HSET in shortening overlaps. Consequently, the increased HSET density in the overlaps leads to a density-dependent decrease in sliding velocity and the generation of an entropic force that antagonizes the force exerted by the motors. Our results demonstrate that a spatial arrangement of microtubules can regulate the collective action of molecular motors through the local alteration of their individual interaction kinetics.
Original languageEnglish
Pages (from-to)1245-1252
Number of pages8
JournalNature Chemical Biology
Volume13
Issue number12
DOIs
Publication statusPublished - 1 Dec 2017

Fingerprint Dive into the research topics of 'Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding'. Together they form a unique fingerprint.

Cite this