NDLI: Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.

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Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.

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Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Aponte, Angel M. Gucek, Marjan Lu, Zhongping Sack, Michael N. Chen, Yong Battaglia, Valentina
Description	Author Affiliation: Lu Z ( From the Cardiovascular and Pulmonary Branch and the Department of Biochemistry and Molecular Medicine, George Washington University, Washington, D. C. 20052, and the Veterans Affairs Medical Center, Washington, D. C. 20422 luz@gwu.edu.); Chen Y ( Proteomic Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.); Aponte AM ( Proteomic Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.); Battaglia V ( the Department of Biochemistry and Molecular Medicine, George Washington University, Washington, D. C. 20052, and the Veterans Affairs Medical Center, Washington, D. C. 20422.); Gucek M ( Proteomic Core Facility, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.); Sack MN ( From the Cardiovascular and Pulmonary Branch and sackm@nih.gov.)
Abstract	Although Sirtuin 3 (SIRT3), a mitochondrially enriched deacetylase and activator of fat oxidation, is down-regulated in response to high fat feeding, the rate of fatty acid oxidation and mitochondrial protein acetylation are invariably enhanced in this dietary milieu. These paradoxical data implicate that additional acetylation modification-dependent levels of regulation may be operational under nutrient excess conditions. Because the heat shock protein (Hsp) Hsp10-Hsp60 chaperone complex mediates folding of the fatty acid oxidation enzyme medium-chain acyl-CoA dehydrogenase, we tested whether acetylation-dependent mitochondrial protein folding contributes to this regulatory discrepancy. We demonstrate that Hsp10 is a functional SIRT3 substrate and that, in response to prolonged fasting, SIRT3 levels modulate mitochondrial protein folding. Acetyl mutagenesis of Hsp10 lysine 56 alters Hsp10-Hsp60 binding, conformation, and protein folding. Consistent with Hsp10-Hsp60 regulation of fatty acid oxidation enzyme integrity, medium-chain acyl-CoA dehydrogenase activity and fat oxidation are elevated by Hsp10 acetylation. These data identify acetyl modification of Hsp10 as a nutrient-sensing regulatory node controlling mitochondrial protein folding and metabolic function.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	4
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-01-23
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chaperonin 10 Metabolism Fasting Protein Folding Sirtuin 3 Acetylation Animals Genetics Chromatography, Gel Electrophoresis, Gel, Two-Dimensional Fatty Acids Flow Cytometry Gene Expression Regulation Mice Mice, Knockout Mitochondria Mitochondrial Proteins Molecular Chaperones Mutagenesis Oxygen Reactive Oxygen Species Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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