The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor alpha  in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

doi:10.1128/MCB.20.5.1868-1876.2000

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Molecular and Cellular Biology, March 2000, p. 1868-1876, Vol. 20, No. 5
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor $alpha$ in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

Rick B. Vega,¹ Janice M. Huss,¹ and Daniel P. Kelly¹^,²^,^*

Center for Cardiovascular Research, Departments of Medicine¹ and Molecular Biology and Pharmacology,² Washington University School of Medicine, St. Louis, Missouri

Received 9 August 1999/Returned for modification 22 September 1999/Accepted 10 December 1999

Peroxisome proliferator-activated receptor $alpha$ (PPAR $alpha$ ) plays a key role in the transcriptional control of genes encoding mitochondrialfatty acid $beta$ -oxidation (FAO) enzymes. In this study we soughtto determine whether the recently identified PPAR gamma coactivator1 (PGC-1) is capable of coactivating PPAR $alpha$ in the transcriptionalcontrol of genes encoding FAO enzymes. Mammalian cell cotransfectionexperiments demonstrated that PGC-1 enhanced PPAR $alpha$ -mediated transcriptionalactivation of reporter plasmids containing PPAR $alpha$ target elements.PGC-1 also enhanced the transactivation activity of a PPAR $alpha$ -Gal4DNA binding domain fusion protein. Retroviral vector-mediatedexpression studies performed in 3T3-L1 cells demonstrated thatPPAR $alpha$ and PGC-1 cooperatively induced the expression of PPAR $alpha$ target genes and increased cellular palmitate oxidation rates.Glutathione S-transferase "pulldown" studies revealed that incontrast to the previously reported ligand-independent interactionwith PPAR $gamma$ , PGC-1 binds PPAR $alpha$ in a ligand-influenced manner. Protein-proteininteraction studies and mammalian cell hybrid experiments demonstratedthat the PGC-1-PPAR $alpha$ interaction involves an LXXLL domain in PGC-1and the PPAR $alpha$ AF2 region, consistent with the observed ligandinfluence. Last, the PGC-1 transactivation domain was mapped towithin the NH₂-terminal 120 amino acids of the PGC-1 molecule,a region distinct from the PPAR $alpha$ interacting domains. These resultsidentify PGC-1 as a coactivator of PPAR $alpha$ in the transcriptionalcontrol of mitochondrial FAO capacity, define separable PPAR $alpha$ interaction and transactivation domains within the PGC-1 molecule,and demonstrate that certain features of the PPAR $alpha$ -PGC-1 interactionare distinct from that of PPAR $gamma$ -PGC-1.

^* Corresponding author. Mailing address: Center for Cardiovascular Research, Washington University School of Medicine, 660 S.Euclid Ave., Campus Box 8086, St. Louis, MO 63110. Phone: (314)362-8908. Fax: (314) 362-0186. E-mail: dkelly{at}imgate.wustl.edu.

Molecular and Cellular Biology, March 2000, p. 1868-1876, Vol. 20, No. 5
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor $alpha$ in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes