Abstract
ABSTRACTDyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest individual component of the dynein complex is the heavy chain. Its C‐terminal 3500 amino‐acid residues form the motor domain, which hydrolyses ATP in its ring of AAA+ (ATPases associated with diverse cellular activities) domains to generate the force for movement. The production of force is synchronized with cycles of microtubule binding and release, another important prerequisite for efficient motility along the microtubule. Although the large scale conformational changes that lead to force production and microtubule affinity regulation are well established, it has been largely enigmatic how ATP‐hydrolysis in the AAA+ ring causes these rearrangements. The past five years have seen a surge of high resolution information on the dynein motor domain that finally allowed unprecedented insights into this important open question. This review, part of the “ATP and GTP hydrolysis in Biology” special issue, will summarize our current understanding of the dynein motor mechanism with a special emphasis on the recently obtained crystal and EM structures. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 557–567, 2016.
Highlights
Dyneins are a large family of motor proteins that harness the energy of ATP-hydrolysis to move along microtubules in the minus end direction
What does the ATP state of the dynein motor look like? What are the molecular interactions at the stalk/buttress interface that drive the sliding of the stalk helices and lead to the change in microtubule affinity? Does linker bending occur in one step or are there discrete substeps? How does microtubule binding trigger the powerstroke? Crystal and electron microscopy structures at higher resolution are needed to answer these questions
The structural analysis presented in this review is based on crystal structures from different dynein isoforms from Saccharomyces cerevisiae, Dictyostelium discoideum, and Homo sapiens
Summary
Division of Structural Studies, Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. Received 8 February 2016; revised 31 March 2016; accepted 1 April 2016 Published online 8 April 2016 in Wiley Online Library (wileyonlinelibrary.com).
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