当前位置： SCI文献检索 > ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS期刊下所有文献 > Regulation of c-Src activity by the expression of wild-type v-Src and its kinase-dead double Y416F-K295N mutant.

Regulation of c-Src activity by the expression of wild-type v-Src and its kinase-dead double Y416F-K295N mutant.

Abstract：

:Active, wild-type v-Src and its kinase-dead double Y416F-K295N mutant were expressed in hamster fibroblasts. Expression of the active v-Src induced activation of endogenous c-Src and increased general protein-tyrosine phosphorylation in the infected cells. Expression of the kinase-dead mutant induced hypophosphorylation of Tyr416 of the endogenous c-Src. The inactivation of c-Src was reversible, as confirmed by in vitro kinase activity of c-Src immunoprecipitated from the kinase-dead v-Src-expressing cells. Both activation and inactivation of c-Src may be explained by direct interaction of the v-Src and c-Src that may either facilitate transphosphorylation of the regulatory Tyr416 in the activation loop, or prevent it by formation of transient dead-end complexes of the Y416F-K295N mutant with c-Src. The interaction was also indicated by co-localization of v- and c-Src proteins in immunofluorescent images of the infected cells. These results suggest that dimerization of Src plays an important role in the regulation of Src tyrosine kinase activity.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Vojtechová M,Senigl F,Sloncová E,Tuhácková Z

doi

10.1016/j.abb.2006.09.011

subject

Has Abstract

pub_date

2006-11-15 00:00:00

pages

136-43

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(06)00348-1

journal_volume

455

pub_type

杂志文章

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