A mitochondrial expatriate: nuclear pyruvate dehydrogenase

Vincent C J de Boer; Sander M Houten

doi:10.1016/j.cell.2014.06.018

A mitochondrial expatriate: nuclear pyruvate dehydrogenase

Cell. 2014 Jul 3;158(1):9-10. doi: 10.1016/j.cell.2014.06.018.

Authors

Vincent C J de Boer¹, Sander M Houten²

Affiliations

¹ Department of Clinical Chemistry, Laboratory Genetic Metabolic Diseases, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; Department of Pediatrics, Emma Children's Hospital, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands. Electronic address: v.c.deboer@amc.uva.nl.
² Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Icahn Institute for Genomics and Multiscale Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA. Electronic address: sander.houten@mssm.edu.

PMID: 24995972
DOI: 10.1016/j.cell.2014.06.018

Abstract

The pyruvate dehydrogenase complex (PDC) catalyzes the conversion of pyruvate into acetyl-CoA, a critical step in metabolism. Sutendra et al. now demonstrate that PDC can translocate from the mitochondria to the nucleus to provide acetyl-CoA necessary for histone acetylation, suggesting a new pathway for mitochondrial-nuclear communication.

Publication types

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MeSH terms

Acetyl Coenzyme A / biosynthesis*
Cell Nucleus / metabolism*
Humans
Pyruvate Dehydrogenase Complex / metabolism*

Substances

Pyruvate Dehydrogenase Complex
Acetyl Coenzyme A