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Updated: Aug 9, 2026

Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
Published on: October 15, 2019
Autoinhibitory and other autoregulatory elements within the dynein motor domain
1Department of Pathology and Cell Biology, Columbia University College of Physicians and Surgeons, P and S 15-410, 630 W. 168th St., New York, NY 10032, USA. rv2025@columbia.edu
Abstract:
The dyneins are a family of microtubule motor proteins. The motor domain, which represents the C-terminal 2/3 of the dynein heavy chain, exhibits homology to the AAA family of ATPases. It consists of a ring of six related but divergent AAA+ units, with two substantial sized protruding projections, the stem, or tail, which anchors the protein to diverse subcellular sites, and the stalk, which binds microtubules. This article reviews recent efforts to probe the mechanism by which the dyneins produce force, and work from the authors' lab regarding long-range conformational regulation of dynein enzymatic activity.
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