Reference: Ecklund KH, et al. (2017) She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain. Nat Commun 8(1):2151

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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.

Reference Type
Journal Article | Research Support, N.I.H., Extramural | Research Support, Non-U.S. Gov't
Authors
Ecklund KH, Morisaki T, Lammers LG, Marzo MG, Stasevich TJ, Markus SM
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