Structural basis for two-way communication between dynein and microtubules

Noritaka Nishida, Yuta Komori, Osamu Takarada, Atsushi Watanabe, Satoko Tamura, Satoshi Kubo, Ichio Shimada () and Masahide Kikkawa ()
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Noritaka Nishida: The University of Tokyo
Yuta Komori: The University of Tokyo
Osamu Takarada: The University of Tokyo
Atsushi Watanabe: The University of Tokyo
Satoko Tamura: The University of Tokyo
Satoshi Kubo: The University of Tokyo
Ichio Shimada: The University of Tokyo
Masahide Kikkawa: The University of Tokyo

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding of the stalk α-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk α-helix even without the disulfide bond, suggesting how the MT-induced conformational changes propagate toward the ATPase domain. Based on differences in the MT-binding surface between the high- and low-affinity states, we propose a potential mechanism for the directional bias of dynein movement on MT tracks.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14842-8

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DOI: 10.1038/s41467-020-14842-8

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