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Structure of dynein–dynactin on microtubules shows tandem adaptor binding

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  • Sami Chaaban

    (Medical Research Council Laboratory of Molecular Biology)

  • Andrew P. Carter

    (Medical Research Council Laboratory of Molecular Biology)

Abstract

Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor1–3. Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour4–6. Different coiled-coil adaptors are linked to different cargos7,8, and some share motifs known to contact sites on dynein and dynactin4,9–13. There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein–dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos.

Suggested Citation

  • Sami Chaaban & Andrew P. Carter, 2022. "Structure of dynein–dynactin on microtubules shows tandem adaptor binding," Nature, Nature, vol. 610(7930), pages 212-216, October.
    • Handle: RePEc:nat:nature:v:610:y:2022:i:7930:d:10.1038_s41586-022-05186-y
    DOI: 10.1038/s41586-022-05186-y
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    Cited by:

    1. Kyoko Okada & Bharat R. Iyer & Lindsay G. Lammers & Pedro A. Gutierrez & Wenzhe Li & Steven M. Markus & Richard J. McKenney, 2023. "Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Yuanchang Zhao & Sena Oten & Ahmet Yildiz, 2023. "Nde1 promotes Lis1-mediated activation of dynein," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Bryan S. Sibert & Joseph Y. Kim & Jie E. Yang & Zunlong Ke & Christopher C. Stobart & Martin L. Moore & Elizabeth R. Wright, 2024. "Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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