Dissecting motility signaling through activation of specific Src-effector complexes.
Nat Chem Biol
; 10(4): 286-90, 2014 Apr.
Article
em En
| MEDLINE
| ID: mdl-24609359
ABSTRACT
We describe an approach to selectively activate a kinase in a specific protein complex or at a specific subcellular location within living cells and within minutes. This reveals the effects of specific kinase pathways without time for genetic compensation. The new technique, dubbed rapamycin-regulated targeted activation of pathways (RapRTAP), was used to dissect the role of Src kinase interactions with FAK and p130Cas in cell motility and morphodynamics. The overall effects of Src activation on cell morphology and adhesion dynamics were first quantified, without restricting effector access. Subsets of Src-induced behaviors were then attributed to specific interactions between Src and the two downstream proteins. Activation of Src in the cytoplasm versus at the cell membrane also produced distinct phenotypes. The conserved nature of the kinase site modified for RapRTAP indicates that the technique can be applied to many kinases.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Quinases
/
Transdução de Sinais
/
Movimento Celular
/
Genes src
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article