She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain

Kari H. Ecklund, Tatsuya Morisaki, Lindsay G. Lammers, Matthew G. Marzo, Timothy J. Stasevich and Steven M. Markus ()
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Kari H. Ecklund: Colorado State University
Tatsuya Morisaki: Colorado State University
Lindsay G. Lammers: Colorado State University
Matthew G. Marzo: Colorado State University
Timothy J. Stasevich: Colorado State University
Steven M. Markus: Colorado State University

Nature Communications, 2017, vol. 8, issue 1, 1-16

Abstract: Abstract Cytoplasmic dynein is an enormous minus end-directed microtubule motor. Rather than existing as bare tracks, microtubules are bound by numerous microtubule-associated proteins (MAPs) that have the capacity to affect various cellular functions, including motor-mediated transport. One such MAP is She1, a dynein effector that polarizes dynein-mediated spindle movements in budding yeast. Here, we characterize the molecular basis by which She1 affects dynein, providing the first such insight into which a MAP can modulate motor motility. We find that She1 affects the ATPase rate, microtubule-binding affinity, and stepping behavior of dynein, and that microtubule binding by She1 is required for its effects on dynein motility. Moreover, we find that She1 directly contacts the microtubule-binding domain of dynein, and that their interaction is sensitive to the nucleotide-bound state of the motor. Our data support a model in which simultaneous interactions between the microtubule and dynein enables She1 to directly affect dynein motility.

Date: 2017
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DOI: 10.1038/s41467-017-02004-2

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