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Oxidation of F-actin controls the terminal steps of cytokinesis

Frémont, Stéphane, Hammich, Hussein, Bai, Jian, Wioland, Hugo, Klinkert, Kerstin, Rocancourt, Murielle, Kikuti, Carlos, Stroebel, David, Romet-Lemonne, Guillaume, Pylypenko, Olena, Houdusse, Anne, Echard, Arnaud·2017·Nature Communications
DOI 10.1038/ncomms14528PMC PMC5331220
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Abstract

Cytokinetic abscission, the terminal step of cell division, crucially depends on the local constriction of ESCRT-III helices after cytoskeleton disassembly. While the microtubules of the intercellular bridge are cut by the ESCRT-associated enzyme Spastin, the mechanism that clears F-actin at the abscission site is unknown. Here we show that oxidation-mediated depolymerization of actin by the redox enzyme MICAL1 is key for ESCRT-III recruitment and successful abscission. MICAL1 is recruited to the abscission site by the Rab35 GTPase through a direct interaction with a flat three-helix domain found in MICAL1 C terminus. Mechanistically, in vitro assays on single actin filaments demonstrate that MICAL1 is activated by Rab35. Moreover, in our experimental conditions, MICAL1 does not act as a severing enzyme, as initially thought, but instead induces F-actin depolymerization from both ends. Our work reveals an unexpected role for oxidoreduction in triggering local actin depolymerization to control a fundamental step of cell division.

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  • In the simplified model, co-residence of TBC1D5 and TBC1D13 to a pseudo-helical Retromer coated tubule would ensure that membrane exiting the retrieval sub-domain has RAB7 in an inactive state (lacks late endosomal identity) and is devoid of active RAB35, restricting association of its effector MICAL1 and preventing F-actin disassembly while simultaneously allowing ARF6 activation to aid recycling

    “The most simplified model to describe a highly dynamic and highly complex set of associations, is that the co-residence of TBC1D5 and TBC1D13 to a pseudo-helical Retromer coated tubule would ensure that membrane exiting the retrieval sub-domain has RAB7 in an inactive state”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [124]

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Research works printed but not linked: 68

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Metadata

Authors
Frémont, S., Hammich, H., Bai, J., Wioland, H., Klinkert, K., Rocancourt, M., Kikuti, C., Stroebel, D., Romet-Lemonne, G., Pylypenko, O., Houdusse, A., & Echard, A.
ORCID
Wioland, Hugo
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2017-02-23
Volume
8
Issue
1
ISSN
2041-1723
DOI
10.1038/ncomms14528
PMC
PMC5331220
Cited by
181
References
2
Language
en
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