Tyrosine Phosphorylation of SGEF Regulates RhoG Activity and Cell Migration.
PLoS One
; 11(7): e0159617, 2016.
Article
em En
| MEDLINE
| ID: mdl-27437949
ABSTRACT
SGEF and Ephexin4 are members of the Ephexin subfamily of RhoGEFs that specifically activate the small GTPase RhoG. It is reported that Ephexin1 and Ephexin5, two well-characterized Ephexin subfamily RhoGEFs, are tyrosine-phosphorylated by Src, and that their phosphorylation affect their activities and functions. In this study, we show that SGEF, but not Ephexin4, is tyrosine-phosphorylated by Src. Tyrosine phosphorylation of SGEF suppresses its interaction with RhoG, the elevation of RhoG activity, and SGEF-mediated promotion of cell migration. We identified tyrosine 530 (Y530), which is located within the Dbl homology domain, as a major phosphorylation site of SGEF by Src, and Y530F mutation blocked the inhibitory effect of Src on SGEF. Taken together, these results suggest that the activity of SGEF is negatively regulated by tyrosine phosphorylation of the DH domain.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Movimento Celular
/
Quinases da Família src
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Proteínas rho de Ligação ao GTP
/
Fatores de Troca do Nucleotídeo Guanina
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article