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.
Original language | English (US) |
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Pages (from-to) | 1466-1473 |
Number of pages | 8 |
Journal | Genes and Development |
Volume | 19 |
Issue number | 12 |
DOIs | |
State | Published - Jun 15 2005 |
Externally published | Yes |
Keywords
- Arginine methylation
- Coactivator
- Mitochondrial biogenesis
- Nuclear receptor
- Transcription
ASJC Scopus subject areas
- General Medicine