期刊
NATURE COMMUNICATIONS
卷 8, 期 -, 页码 1-16出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms14528
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资金
- Institut Pasteur
- CNRS
- FRM [Equipe FRM DEQ20120323707, FDT20150532389]
- INCa [2014-1-PL BIO-04-IP1, 2014-1-PL BIO-04-ICR-1]
- ANR (AbCyStem)
- IXCORE foundation
- Pasteur Paris Universites International PhD program
- Carnot-Pasteur MI
- PSL Universite
- Fondation ARC pour la recherche sur le cancer
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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