Direct redox regulation of F-actin assembly and disassembly by Mical

Ruei Jiun Hung, Chi W. Pak, Jonathan R. Terman

Research output: Contribution to journalArticle

165 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1710-1713
Number of pages4
JournalScience
Volume334
Issue number6063
DOIs
StatePublished - Dec 23 2011

ASJC Scopus subject areas

  • General

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