Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8298861 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2010 | 10 Pages |
Abstract
Work is presented on the role of cAMP-dependent protein phosphorylation in post-translational processing and biosynthesis of complex I subunits in mammalian cell cultures. PKA-mediated phosphorylation of the NDUFS4 subunit of complex I promotes in cell cultures in vivo import/maturation in mitochondria of the precursor of this protein. The import promotion appears to be associated with the observed cAMP-dependent stimulation of the catalytic activity of complex I. These effects of PKA are counteracted by activation of protein phosphatase(s). PKA and the transcription factor CREB play a critical role in the biosynthesis of complex I subunits. CREB phosphorylation, by PKA and/or CaMKs, activates at nuclear and mitochondrial level a transcriptional regulatory cascade which promotes the concerted expression of nuclear and mitochondrial encoded subunits of complex I and other respiratory chain proteins.
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Authors
Sergio Papa, Salvatore Scacco, Domenico De Rasmo, Anna Signorile, Francesco Papa, Damiano Panelli, Annarita Nicastro, Raffaella Scaringi, Arcangela Santeramo, Emilio Roca, Raffaella Trentadue, Maria Larizza,