Activation of nuclear receptor coactivator PGC-1α by arginine methylation
Abstract
Peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α), a tissue-specific and inducible transcriptional coactivator for several nuclear receptors, plays a key role in energy metabolism. We report here that PGC-1α coactivator activity is potentiated by arginine methylation by protein arginine methyltransferase 1 (PRMT1), another nuclear receptor coactivator. Mutation of three substrate arginines in the C-terminal region of PGC-1α abolished the cooperative coactivator function of PGC-1α and PRMT1, and compromised the ability of PGC-1α to induce endogenous target genes. Finally, endogenous PRMT1 contributes to PGC-1α coactivator activity, and to the induction of genes important for mitochondrial biogenesis.
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Footnotes
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Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1295005.
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Corresponding authors.
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↵3 Present address: INSERM EMI 229, Centre de Recherche en Cancérologie, 34298 Monpellier, Cedex 05, France.
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↵4 E-MAIL kralli{at}scripps.edu; FAX (858) 784-9132.
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↵5 E-MAIL stallcup{at}usc.edu; FAX (323) 442-3049.
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- Accepted May 3, 2005.
- Received January 3, 2005.
- Cold Spring Harbor Laboratory Press