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Activation of cytoplasmic dynein through microtubule crossbridging

View ORCID ProfileManas Chakraborty, View ORCID ProfileAlgirdas Toleikis, View ORCID ProfileNida Siddiqui, View ORCID ProfileRobert A. Cross, View ORCID ProfileAnne Straube
doi: https://doi.org/10.1101/2020.04.13.038950
Manas Chakraborty
Centre for Mechanochemical Cell Biology & Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK
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Algirdas Toleikis
Centre for Mechanochemical Cell Biology & Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK
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Nida Siddiqui
Centre for Mechanochemical Cell Biology & Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK
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Robert A. Cross
Centre for Mechanochemical Cell Biology & Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK
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Anne Straube
Centre for Mechanochemical Cell Biology & Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK
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  • For correspondence: anne@mechanochemistry.org
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Summary

Cytoplasmic dynein is the main microtubule-minus-end-directed transporter of cellular cargo in animal cells [1, 2]. Cytoplasmic dynein also functions in the organisation and positioning of mitotic spindles [3, 4] and the formation of ordered microtubule arrays in neurons and muscle [5, 6]. Activation of the motor for cargo transport is thought to require formation of a complex with dynactin and a cargo adapter [7-10]. Here we show that recombinant human dynein can crossbridge neighbouring microtubules and can be activated by this crossbridging to slide and polarity-sort microtubule bundles. While single molecules of human dynein are predominantly static or diffusive on single microtubules, they walk processively for 1.5 μm on average along the microtubule bundles they form. Speed and force output of dynein are doubled on bundles compared to single microtubules, indicating that the crossbridging dynein steps equivalently on two microtubules. Our data are consistent with a model of autoactivation through the physical separation of dynein motor domains when crossbridging two microtubules. This enables cytoplasmic dynein to function effectively as a microtubule organiser and transporter without needing to first form a complex with dynactin and a cargo adapter.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted April 13, 2020.
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Activation of cytoplasmic dynein through microtubule crossbridging
Manas Chakraborty, Algirdas Toleikis, Nida Siddiqui, Robert A. Cross, Anne Straube
bioRxiv 2020.04.13.038950; doi: https://doi.org/10.1101/2020.04.13.038950
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Activation of cytoplasmic dynein through microtubule crossbridging
Manas Chakraborty, Algirdas Toleikis, Nida Siddiqui, Robert A. Cross, Anne Straube
bioRxiv 2020.04.13.038950; doi: https://doi.org/10.1101/2020.04.13.038950

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