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Published on: February 27, 2016
The pyruvate dehydrogenase complex at the epigenetic crossroads of acetylation and lactylation
Peter W Stacpoole1, Carolyn O Dirain2
1University of Florida, College of Medicine Department of Medicine, Department of Biochemistry & Molecular Biology, Gainesville, FL, United States.
Abstract:
The pyruvate dehydrogenase complex (PDC) is remarkable for its size and structure as well as for its physiological and pathological importance. Its canonical location is in the mitochondrial matrix, where it primes the tricarboxylic acid (TCA) cycle by decarboxylating glycolytically-derived pyruvate to acetyl-CoA. Less well appreciated is its role in helping to shape the epigenetic landscape, from early development throughout mammalian life by its ability to "moonlight" in the nucleus, with major repercussions for human healthspan and lifespan. The PDC's influence on two crucial modifiers of the epigenome, acetylation and lactylation, is the focus of this brief review.
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