Oxidation of F-actin controls the terminal steps of cytokinesis - Sorbonne Université Access content directly
Journal Articles Nature Communications Year : 2017

Oxidation of F-actin controls the terminal steps of cytokinesis

Hugo Wioland
Carlos Kikuti
Olena Pylypenko
Anne Houdusse


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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Dates and versions

hal-01492528 , version 1 (20-03-2017)





Stéphane Frémont, Hussein Hammich, Jian Bai, Hugo Wioland, Kerstin Klinkert, et al.. Oxidation of F-actin controls the terminal steps of cytokinesis. Nature Communications, 2017, 8, pp.1-16. ⟨10.1038/ncomms14528⟩. ⟨hal-01492528⟩
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