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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Frémont S,Hammich H,Bai J,Wioland H,Klinkert K,Rocancourt M,Kikuti C,Stroebel D,Romet-Lemonne G,Pylypenko O,Houdusse A,Echard Adoi
10.1038/ncomms14528subject
Has Abstractpub_date
2017-02-23 00:00:00pages
14528issn
2041-1723pii
ncomms14528journal_volume
8pub_type
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