Regulation by the autophosphorylation site in overexpressed pp60c-src.
AUTOR(ES)
Kmiecik, T E
RESUMO
We show that overexpressed pp60c-src is phosphorylated at Tyr-416 and has increased specific kinase activity when isolated from cells incubated with vanadate, a tyrosine phosphatase inhibitor. This supports the hypothesis that transient Tyr-416 phosphorylation modulates the activity of overexpressed pp60c-src in vivo. Mutagenesis indicates that Tyr-416 modulates pp60v-src activity as well.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=365532Documentos Relacionados
- Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src.
- Tyrosine phosphorylation of G protein alpha subunits by pp60c-src.
- Neural tissues express high levels of the cellular src gene product pp60c-src.
- Phosphorylation of tyrosine in the carboxyl-terminal tryptic peptide of pp60c-src.
- Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src.