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Updated: Jun 2, 2025

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
Published on: March 15, 2014
Molecular basis for the assembly of the dynein transport machinery on microtubules
Qinhui Rao1, Pengxin Chai1, Kai Zhang1
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA.
Abstract:
Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has been elusive. Here, we reveal detailed structural insights into microtubule-mediated DDA assembly using cryo-electron microscopy. We find that an adaptor-independent dynein-dynactin complex (DD) predominantly forms on microtubules in an intrinsic 2:1 stoichiometry, induced by spontaneous parallelization of dynein upon microtubule binding. Adaptors can squeeze in and exchange within the assembled microtubule-bound DD complex, which is enabled by relative rotations between dynein and dynactin, and further facilitated by dynein light intermediate chains that assist in an adaptor 'search' mechanism. Our findings elucidate the dynamic adaptability of the dynein transport machinery, and reveal a new mode for assembly of the motile complex.
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