Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement

BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology
Helgo Schmidt

Abstract

Dyneins are a family of motor proteins that move along the microtubule. Motility is generated in the motor domain, which consists of a ring of six AAA+ (ATPases associated with diverse cellular activities) domains, the linker and the microtubule-binding domain (MTBD). The cyclic ATP-hydrolysis in the AAA+ ring causes the remodelling of the linker, which creates the necessary force for movement. The production of force has to be synchronized with cycles of microtubule detachment and rebinding to efficiently create movement along the microtubule. The analysis of four dynein motor domain crystal structures in the essay presented here provides evidence that this crucial coordination is carried out by open/closed AAA+ ring conformations.

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Dec 19, 2015·Trends in Biochemical Sciences·Gira BhabhaRonald D Vale
Oct 21, 2015·The Journal of Cell Biology·Lindsay G Lammers, Steven M Markus
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