title: Redox switch for actin.
abstract: Oxidation of actin methionine residues by the oxidation-reduction enzyme Mical is known to lead to actin filament depolymerization. SelR enzymes are now shown to reduce these oxidized actin methionines, revealing a regulated redox reaction mechanism through which cells control the assembly and disassembly of actin filaments.
authors.affiliation: Heinrich-Heine-Universität Düsseldorf, AG Funktionelle Zellmorphologie, Universitätsstraße 1, Geb. 26-12-00, 40223 Düsseldorf, Germany.
authors.forename: Hermann
authors.initials: H
authors.lastname: Aberle
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D004268:DNA-Binding Proteins / Q000378:metabolism*; D029721:Drosophila Proteins / Q000502:physiology*; D004331:Drosophila melanogaster / Q000166:cytology*; D005260:Female; D008297:Male; D051150:Methionine Sulfoxide Reductases / Q000502:physiology*
chemical_list: D000199:Actins; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; C496247:MICAL protein, Drosophila; D051150:Methionine Sulfoxide Reductases; C495234:SelR protein, Drosophila