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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAUFWWxxH-udYkzWyEgo5PkvHbJ86hZuclVWEZluYQQZI#_6 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAUFWWxxH-udYkzWyEgo5PkvHbJ86hZuclVWEZluYQQZI#_5 http://www.w3.org/ns/prov#value Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. 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