Abstract
Dynein is an AAA+ type motor complex that utilizes ATP hydrolysis to move toward the minus end of microtubules. Mechanistic studies on dynein have been hampered by its enormous size (a molecular mass of > 1 MDa) and molecular complexity. However, recent advances in structural and functional studies, including electron microscopic observations and mutational analyses along with establishment of recombinant expression systems, are now beginning to shed light on the molecular mechanism of dynein. Here, I summarize these recent studies, focusing on the coupling between ATP hydrolysis cycle and conformational changes that is critical for the dynein-based motility.
