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. 2013 Dec 15;126(24):5657–5669. doi: 10.1242/jcs.133819

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© 2013. Published by The Company of Biologists Ltd

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Fig. 4. — PKCε-mediated phosphorylation of INrf2S602, INrf2−Nrf2 interaction and Nrf2 degradation in PKCε^+/+ and PKC^−/− MEFs. (A) Immunoblot analysis of PKCε levels in PKCε^+/+ and PKCε^−/− MEFs. (B) INrf2 serine phosphorylation analysis. INrf2-V5 and mutant INrf2S602A-V5 plasmids were transfected into PKCε^+/+ and PKCε^−/− MEFs and INrf2 serine phosphorylation was analyzed by reciprocal immunoprecipitation and immunoblotting. (C) Interaction of INrf2-V5 and mutant INrf2S602A-V5 with FLAG-Nrf2 was analyzed in the PKCε^+/+ and PKCε^−/− MEFs after transfection of indicated plasmids by reciprocal immunoprecipitation and immunoblotting using specific antibodies (left panels). Nrf2 ubiquitylation was analyzed from PKCε^+/+ and PKCε^−/− cells transfected with INrf2 and mutant INrf2S602A as indicated (right panels). (D) PKCε^−/− MEFs were co-transfected with INrf2-V5 or mutant INrf2S602A-V5 plasmids with pcDNA or FLAG-PKCε and INrf2 serine phosphorylation and interaction with Nrf2 was analyzed by immunoprecipitation and immunoblotting using specific antibodies. (E) PKCε^+/+ and PKCε^−/− cells were transfected with INrf2-V5 and mutant INrf2S602A-V5 plasmids and interaction of INrf2 and mutant INrf2 with Nrf2 and INrf2 known interacting partners was analyzed by immunoprecipitation and immunoblotting.