Direct Redox Regulation of F-Actin Assembly and Disassembly by Mical
- 23 December 2011
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 334 (6063), 1710-1713
- https://doi.org/10.1126/science.1211956
Abstract
Different types of cell behavior, including growth, motility, and navigation, require actin proteins to assemble into filaments. Here, we describe a biochemical process that was able to disassemble actin filaments and limit their reassembly. Actin was a specific substrate of the multidomain oxidation-reduction enzyme, Mical, a poorly understood actin disassembly factor that directly responds to Semaphorin/Plexin extracellular repulsive cues. Actin filament subunits were directly modified by Mical on their conserved pointed-end, which is critical for filament assembly. Mical posttranslationally oxidized the methionine 44 residue within the D-loop of actin, simultaneously severing filaments and decreasing polymerization. This mechanism underlying actin cytoskeletal collapse may have broad physiological and pathological ramifications.Keywords
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