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

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 Commun

journal_title

Nature communications

authors

Frémont S,Hammich H,Bai J,Wioland H,Klinkert K,Rocancourt M,Kikuti C,Stroebel D,Romet-Lemonne G,Pylypenko O,Houdusse A,Echard A

doi

10.1038/ncomms14528

subject

Has Abstract

pub_date

2017-02-23 00:00:00

pages

14528

issn

2041-1723

pii

ncomms14528

journal_volume

8

pub_type

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