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The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein

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  • Xinglei Liu

    (Albert Einstein College of Medicine)

  • Lu Rao

    (Albert Einstein College of Medicine)

  • Arne Gennerich

    (Albert Einstein College of Medicine)

Abstract

Cytoplasmic dynein is the primary motor for microtubule minus-end-directed transport and is indispensable to eukaryotic cells. Although each motor domain of dynein contains three active AAA+ ATPases (AAA1, 3, and 4), only the functions of AAA1 and 3 are known. Here, we use single-molecule fluorescence and optical tweezers studies to elucidate the role of AAA4 in dynein’s mechanochemical cycle. We demonstrate that AAA4 controls the priming stroke of the motion-generating linker, which connects the dimerizing tail of the motor to the AAA+ ring. Before ATP binds to AAA4, dynein remains incapable of generating motion. However, when AAA4 is bound to ATP, the gating of AAA1 by AAA3 prevails and dynein motion can occur. Thus, AAA1, 3, and 4 work together to regulate dynein function. Our work elucidates an essential role for AAA4 in dynein’s stepping cycle and underscores the complexity and crosstalk among the motor’s multiple AAA+ domains.

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  • Xinglei Liu & Lu Rao & Arne Gennerich, 2020. "The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein," Nature Communications, Nature, vol. 11(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19477-3
    DOI: 10.1038/s41467-020-19477-3
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    Cited by:

    1. Xinglei Liu & Lu Rao & Weihong Qiu & Florian Berger & Arne Gennerich, 2024. "Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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