5LE0

MICAL1 Cterminal domain

Summary for 5LE0

• Entry DOI: 10.2210/pdb5le0/pdb
• Descriptor: Protein-methionine sulfoxide oxidase MICAL1 (1 entity in total)
• Functional Keywords: mical, oxidoreductase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: Q8TDZ2
• Total number of polymer chains: 1
• Total formula weight: 17666.59

Authors

Hammich, H.,Pylypenko, O.,Houdusse, A. (deposition date: 2016-06-29, release date: 2017-03-01, Last modification date: 2024-11-13)

Primary citation

Fremont, S.,Hammich, H.,Bai, J.,Wioland, H.,Klinkert, K.,Rocancourt, M.,Kikuti, C.,Stroebel, D.,Romet-Lemonne, G.,Pylypenko, O.,Houdusse, A.,Echard, A.
Oxidation of F-actin controls the terminal steps of cytokinesis.
Nat Commun, 8:14528-14528, 2017

PubMed 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.

PubMed: 28230050
DOI: 10.1038/ncomms14528

Experimental method

X-RAY DIFFRACTION (3.3 Å)