ATP-driven Remodeling of the Linker Domain in the Dynein Motor

Overview

Journal Structure

Publisher Cell Press

Specialties Biochemistry
Biotechnology
Cell Biology
Molecular Biology

Date 2012 Aug 7

PMID 22863569

Citations 48

Authors

Anthony J Roberts

Bara Malkova

Matt L Walker

Hitoshi Sakakibara

Naoki Numata

Takahide Kon

Reiko Ohkura

Thomas A Edwards

Peter J Knight

Kazuo Sutoh

Kazuhiro Oiwa

Stan A Burgess

Affiliations

Soon will be listed here.

Abstract

Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped enzymes, but how they harness this architecture to produce movement is poorly understood. Here, we have used cryo-EM to determine 3D maps of native flagellar dynein-c and a cytoplasmic dynein motor domain in different nucleotide states. The structures show key sites of conformational change within the AAA+ ring and a large rearrangement of the "linker" domain, involving a hinge near its middle. Analysis of a mutant in which the linker "undocks" from the ring indicates that linker remodeling requires energy that is supplied by interactions with the AAA+ modules. Fitting the dynein-c structures into flagellar tomograms suggests how this mechanism could drive sliding between microtubules, and also has implications for cytoplasmic cargo transport.

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