Journal
MOLECULAR CELL
Volume 12, Issue 5, Pages 1137-1149Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(03)00391-5
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Funding
- NATIONAL CANCER INSTITUTE [R35CA042567] Funding Source: NIH RePORTER
- NCI NIH HHS [CA42567] Funding Source: Medline
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Transcriptional coactivators; showing physical and functional interactions with PPARgamma include the protein acetyl transferase p300, the TRAP/Mediator complex that interacts with the general transcription machinery, and the highly regulated PGC-1alpha. We show that PGC-1alpha directly interacts with TRAP/Mediator, through the PPARgamma-interacting subunit TRAP220, and stimulates TRAP/Mediator-dependent function on DNA templates. Further, while ineffective by itself, PGC-1alpha stimulates p300-dependent histone acetylation and transcription on chromatin templates in response to PPARgamma. These functions are mediated by largely independent PPARgamma, p300, and TRAP220 interaction domains in PGC-1alpha, whereas p300 and TRAP220 show ligand-dependent interactions with a common region of PPARgamma. Apart from showing PGC-1alpha functions both in chromatin remodeling and in preinitiation complex formation or function (transcription), these results suggest a key role for PGC-1alpha, through concerted but dynamic interactions, in coordinating these steps.
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