Oxidation of F-actin controls the terminal steps of cytokinesis

Stéphane Frémont, Hussein Hammich, Jian Bai, Hugo Wioland, Kerstin Klinkert, Murielle Rocancourt, Carlos Kikuti, David Stroebel, Guillaume Romet-Lemonne, Olena Pylypenko, Anne Houdusse and Arnaud Echard ()
Additional contact information
Stéphane Frémont: Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department Institut Pasteur
Hussein Hammich: Structural Motility, Institut Curie, PSL Research University,
Jian Bai: Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department Institut Pasteur
Hugo Wioland: Institut Jacques Monod, CNRS, Université Paris Diderot, Université Sorbonne Paris Cité
Kerstin Klinkert: Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department Institut Pasteur
Murielle Rocancourt: Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department Institut Pasteur
Carlos Kikuti: Structural Motility, Institut Curie, PSL Research University,
David Stroebel: Ecole Normale Supérieure, PSL Research University, CNRS, INSERM, Institut de Biologie de l'École Normale Supérieure (IBENS)
Guillaume Romet-Lemonne: Institut Jacques Monod, CNRS, Université Paris Diderot, Université Sorbonne Paris Cité
Olena Pylypenko: Structural Motility, Institut Curie, PSL Research University,
Anne Houdusse: Structural Motility, Institut Curie, PSL Research University,
Arnaud Echard: Membrane Traffic and Cell Division Lab, Cell Biology and Infection Department Institut Pasteur

Nature Communications, 2017, vol. 8, issue 1, 1-16

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/ncomms14528 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14528

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms14528

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().