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Ahnak Protein Activates Protein Kinase C (PKC) through Dissociation of the PKC-Protein Phosphatase 2A Complex
DC Field | Value | Language |
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dc.contributor.author | Lee, In Hye | - |
dc.contributor.author | Lim, Hee Jung | - |
dc.contributor.author | Yoon, Suhyeon | - |
dc.contributor.author | Sung, Je Kyeong | - |
dc.contributor.author | Bae, Duk Soo | - |
dc.contributor.author | Rhee, Sue Goo | - |
dc.contributor.author | Bae, Yun Soo | - |
dc.date.accessioned | 2009-08-25T07:34:37Z | - |
dc.date.available | 2009-08-25T07:34:37Z | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | J. Biol. Chem. 283, 6312-6320 | en |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://hdl.handle.net/10371/7776 | - |
dc.description.abstract | We have previously reported that central repeated units (CRUs) of Ahnak act as a scaffolding protein networking phospholipase C and protein kinase C (PKC). Here, we demonstrate that an Ahnak derivative consisting of four central repeated units binds and activates PKC- 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- 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- activity is regulated through association with protein phosphatase 2A (PP2A). A co-immunoprecipitation assay indicated that the association of PKC- 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. | en |
dc.description.sponsorship | This work was supported in part by the National Core Research Center program
of the Ministry of Science and Technology/Korea Science and Engineering Foundation (Grant R15-2006-020-00000-0) through the Center for Cell Signaling and Drug Discovery Research at Ewha Womans University, Basic Research Program of the Korea Science and Engineering Foundation Grant RO1-2005-000-10480-0 (to Y. S. B.), and 21C Frontier Functional Proteomics Projects Grant FPR0502-470 (to S. G. R.). | en |
dc.language.iso | en | en |
dc.publisher | American Society for Biochemistry and Molecular Biology | en |
dc.title | Ahnak Protein Activates Protein Kinase C (PKC) through Dissociation of the PKC-Protein Phosphatase 2A Complex | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 이인혜 | - |
dc.contributor.AlternativeAuthor | 임희정 | - |
dc.contributor.AlternativeAuthor | 윤수현 | - |
dc.contributor.AlternativeAuthor | 성제경 | - |
dc.contributor.AlternativeAuthor | 배덕수 | - |
dc.contributor.AlternativeAuthor | 이수구 | - |
dc.contributor.AlternativeAuthor | 배윤수 | - |
dc.identifier.doi | 10.1074/jbc.M706878200 | - |
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