Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 1, Pages 94-105Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2015.11.004
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Funding
- NIH [R01GM09731, K99GM112982]
- California Institute for Quantitative Biosciences, qb3@UCSF
- UCSF School of Pharmacy, Mary Anne Koda-Kimble Seed Award for Innovation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [K99GM112982, R01GM097312] Funding Source: NIH RePORTER
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Cytoplasmic dynein, a member of the AAA (ATPases Associated with diverse cellular Activities) family of proteins, drives the processive movement of numerous intracellular cargos towards the minus end of microtubules. Here, we summarize the structural and motile properties of dynein and highlight features that distinguish this motor from kinesin-1 and myosin V, two well-studied transport motors. Integrating information from recent crystal and cryoelectron microscopy structures, as well as high-resolution single-molecule studies, we also discuss models for how dynein biases its movement in one direction along a microtubule track, and present a movie that illustrates these principles.
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