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Tension on the linker gates the ATP-dependent release of dynein from microtubules

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Listed:
  • Frank B. Cleary

    (Biophysics Graduate Group, University of California)

  • Mark A. Dewitt

    (Biophysics Graduate Group, University of California)

  • Thomas Bilyard

    (University of California)

  • Zaw Min Htet

    (University of California)

  • Vladislav Belyy

    (Biophysics Graduate Group, University of California)

  • Danna D. Chan

    (University of California)

  • Amy Y. Chang

    (University of California)

  • Ahmet Yildiz

    (University of California)

Abstract

Cytoplasmic dynein is a dimeric motor that transports intracellular cargoes towards the minus end of microtubules (MTs). In contrast to other processive motors, stepping of the dynein motor domains (heads) is not precisely coordinated. Therefore, the mechanism of dynein processivity remains unclear. Here, by engineering the mechanical and catalytic properties of the motor, we show that dynein processivity minimally requires a single active head and a second inert MT-binding domain. Processivity arises from a high ratio of MT-bound to unbound time, and not from interhead communication. In addition, nucleotide-dependent microtubule release is gated by tension on the linker domain. Intramolecular tension sensing is observed in dynein’s stepping motion at high interhead separations. On the basis of these results, we propose a quantitative model for the stepping characteristics of dynein and its response to chemical and mechanical perturbation.

Suggested Citation

  • Frank B. Cleary & Mark A. Dewitt & Thomas Bilyard & Zaw Min Htet & Vladislav Belyy & Danna D. Chan & Amy Y. Chang & Ahmet Yildiz, 2014. "Tension on the linker gates the ATP-dependent release of dynein from microtubules," Nature Communications, Nature, vol. 5(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5587
    DOI: 10.1038/ncomms5587
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