Vliv exprese divoké a kinázově mrtvé dvojité Y416F-K295N mutované formy v-Src na regulaci aktivity c-Src

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F06%3A00048926" target="_blank" >RIV/68378050:_____/06:00048926 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

Wild-type v-Src and its kinase-dead double Y416F-K295N mutant were expressed in hamster fibroblasts. Wild-type v-Src expression induced activation of endogenous c-Src and increased protein-tyrosine phosphorylation in the infected cells. Expression of thekinase-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 activationand inactivation of c-Src may be explained by direct interaction of the v-Src and c-Src that may either facilitate transphosphorylation of 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, confirmed by co-localization of both Src proteins in immunofluorescent images of the infected cells, suggests that dimerization of Src plays is important in the regulation of Src kinase activity.

Název v anglickém jazyce

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

Popis výsledku anglicky

Wild-type v-Src and its kinase-dead double Y416F-K295N mutant were expressed in hamster fibroblasts. Wild-type v-Src expression induced activation of endogenous c-Src and increased protein-tyrosine phosphorylation in the infected cells. Expression of thekinase-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 activationand inactivation of c-Src may be explained by direct interaction of the v-Src and c-Src that may either facilitate transphosphorylation of 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, confirmed by co-localization of both Src proteins in immunofluorescent images of the infected cells, suggests that dimerization of Src plays is important in the regulation of Src kinase activity.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2006

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Archives of Biochemistry and Biophysics

ISSN

0003-9861

e-ISSN

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Svazek periodika

455

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

136-143

Kód UT WoS článku

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EID výsledku v databázi Scopus

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