View : 191 Download: 122

Full metadata record

DC Field Value Language
dc.contributor.author이서구-
dc.contributor.author배윤수-
dc.contributor.author이인혜-
dc.date.accessioned2016-08-28T12:08:53Z-
dc.date.available2016-08-28T12:08:53Z-
dc.date.issued2008-
dc.identifier.issn0021-9258-
dc.identifier.otherOAK-4653-
dc.identifier.urihttp://dspace.ewha.ac.kr/handle/2015.oak/219966-
dc.description.abstractWe have previously reported that central repeated units (CRUs) of Ahnak act as a scaffolding protein networking phospholipase Cγ and protein kinase C (PKC). Here, we demonstrate that an Ahnak derivative consisting of four central repeated units binds and activates PKC-α in a phosphatidylserine/1,2- dioleoyl-sn-glycerol-independent manner. Moreover, NIH3T3 cells expressing the 4 CRUs of Ahnak showed enhanced c-Raf, MEK, and Erk phosphorylation in response to phorbol 12-myristate 13-acetate (PMA) compared with parental cells. To evaluate the effect of loss-of-function of Ahnak in cell signaling, we investigated PKC activation and Raf phosphorylation in embryonic fibroblast cells (MEFs) of the Ahnak knock-out (Ahnak-/-) mouse. Membrane translocation of PKC-α and phosphorylation of Raf in response to PMA or platelet-derived growth factor were decreased in Ahnak null MEF cells compared with wild type MEFs. Several lines of evidence suggest that PKC-α activity is regulated through association with protein phosphatase 2A (PP2A). A co-immunoprecipitation assay indicated that the association of PKC-α with PP2A was disrupted in NIH3T3 cells expressing 4 CRUs of Ahnak in response to PMA. Consistently, Ahnak null MEF cells stimulated by PMA showed enhanced PKC-PP2A complex formation, and add-back expression of Ahnak into Ahnak null MEF cells abolished the PKC-PP2A complex formation in response to PMA. These data indicate that Ahnak potentiates PKC activation through inhibiting the interaction of PKC with PP2A. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.languageEnglish-
dc.titleAhnak protein activates protein kinase C (PKC) through dissociation of the PKC-protein phosphatase 2A complex-
dc.typeArticle-
dc.relation.issue10-
dc.relation.volume283-
dc.relation.indexSCI-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage6312-
dc.relation.lastpage6320-
dc.relation.journaltitleJournal of Biological Chemistry-
dc.identifier.doi10.1074/jbc.M706878200-
dc.identifier.wosidWOS:000253779500038-
dc.identifier.scopusid2-s2.0-44449175698-
dc.author.googleIn H.L.-
dc.author.googleHee J.L.-
dc.author.googleYoon S.-
dc.author.googleJe K.S.-
dc.author.googleDuk S.B.-
dc.author.googleSue G.R.-
dc.author.googleYun S.B.-
dc.contributor.scopusid이서구(7401852092;25923074700)-
dc.contributor.scopusid배윤수(15031067200)-
dc.contributor.scopusid이인혜(26531358400)-
dc.date.modifydate20190901081003-


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE