SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics.
Nat Cell Biol
; 15(12): 1445-54, 2013 Dec.
Article
em En
| MEDLINE
| ID: mdl-24212093
Actin's polymerization properties are markedly altered by oxidation of its conserved Met 44 residue. Mediating this effect is a specific oxidation-reduction (redox) enzyme, Mical, that works with Semaphorin repulsive guidance cues and selectively oxidizes Met 44. We now find that this actin-regulatory process is reversible. Employing a genetic approach, we identified a specific methionine sulfoxide reductase (MsrB) enzyme SelR that opposes Mical redox activity and Semaphorin-Plexin repulsion to direct multiple actin-dependent cellular behaviours in vivo. SelR specifically catalyses the reduction of the R isomer of methionine sulfoxide (methionine-R-sulfoxide) to methionine, and we found that SelR directly reduced Mical-oxidized actin, restoring its normal polymerization properties. These results indicate that Mical oxidizes actin stereospecifically to generate actin Met-44-R-sulfoxide (actin(Met(R)O-44)), and also implicate the interconversion of specific Met/Met(R)O residues as a precise means to modulate protein function. Our results therefore uncover a specific reversible redox actin regulatory system that controls cell and developmental biology.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Actinas
/
Proteínas de Drosophila
/
Proteínas de Ligação a DNA
/
Drosophila melanogaster
/
Metionina Sulfóxido Redutases
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article