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Nat Commun. 2017 Feb 23;8:14528. doi: 10.1038/ncomms14528.

Oxidation of F-actin controls the terminal steps of cytokinesis.

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Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris Cedex 15, France.
Centre National de la Recherche Scientifique UMR3691, 75015 Paris, France.
Structural Motility, Institut Curie, PSL Research University, CNRS, UMR 144, F-75005 Paris, France.
Sorbonne Universités, UPMC Univ Paris06, Sorbonne Universités, IFD, 4 Place Jussieu, 75252 Paris Cedex 15, France.
Institut Jacques Monod, CNRS, Université Paris Diderot, Université Sorbonne Paris Cité, 75013 Paris, France.
Ecole Normale Supérieure, PSL Research University, CNRS, INSERM, Institut de Biologie de l'École Normale Supérieure (IBENS), 75005 Paris, France.


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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