Report

Activation of PPARγ Coactivator-1 Through Transcription Factor Docking

Science  12 Nov 1999:
Vol. 286, Issue 5443, pp. 1368-1371
DOI: 10.1126/science.286.5443.1368

You are currently viewing the abstract.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


Abstract

Transcriptional coactivators have been viewed as constitutively active components, using transcription factors mainly to localize their functions. Here, it is shown that PPARγ coactivator–1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator–1 (SRC-1) and CREB binding protein (CBP)/p300. PGC-1 has a low inherent transcriptional activity when it is not bound to a transcription factor. The docking of PGC-1 to peroxisome proliferator-activated receptor γ (PPARγ) stimulates an apparent conformational change in PGC-1 that permits binding of SRC-1 and CBP/p300, resulting in a large increase in transcriptional activity. Thus, transcription factor docking switches on the activity of a coactivator protein.

  • * To whom correspondence should be addressed. E-mail: bruce_spiegelman{at}dfci.harvard.edu

View Full Text

Cited By...