RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/24212093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24212093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24212093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/24212093http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.org/dc/terms/identifier"doi:10.1038/ncb2871"xsd:string
http://purl.uniprot.org/citations/24212093http://purl.org/dc/terms/identifier"doi:10.1038/ncb2871"xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Hung R.J."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Hung R.J."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Terman J.R."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Terman J.R."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Yesilyurt H.G."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Yesilyurt H.G."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Spaeth C.S."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/author"Spaeth C.S."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/pages"1445-1454"xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/pages"1445-1454"xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/title"SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/title"SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics."xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/24212093http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/24212093http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24212093