Journal
SCIENCE
Volume 334, Issue 6063, Pages 1710-1713Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1211956
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Funding
- Cancer Prevention Research Institute of Texas (CPRIT)
- NIH [DK091074, NS073968]
- Welch Foundation [I-1749]
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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.
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