Oxidation of F-actin controls the terminal steps of cytokinesis

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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

Edité par CCSD ; Nature Publishing Group -

International audience. 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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