Abstract
Dynein is a minus-end-directed microtubule motor protein that powers the beating of cilia and flagella and transports a wide variety of cargoes within the cytoplasm of eukaryotic cells. Dynein is not evolutionarily related to the cytoskeletal motor proteins kinesin and myosin, but instead is a member of the AAA+ superfamily. Unlike most AAA+ ATPases that self-assemble into homo-hexameric rings, dynein has six distinct AAA+ domains that are concatenated within a single, large polypeptide chain; extending from one of the AAA+ domains is a long, anti-parallel coiled-coil extension (called the stalk) that binds to microtubules. We have studied the mechanism of dynein motility using a combination of structural and single molecule studies. I will discuss how the two motor domains of dynein can act to slide apart anti-parallel microtubules, an activity that may be important for dynein's actions in organizing the mitotic spindle during mitosis. I also will discuss how dynein's enzymatic cycle might be regulated for normal cargo transport.
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