Activation of PPARγ coactivator-1 through transcription factor docking

Pere Puigserver; Guillaume Adelmant; Zhidan Wu; Melina Fan; Jianming Xu; Bert O'Malley; Bruce M. Spiegelman

doi:10.1126/science.286.5443.1368

Activation of PPARγ coactivator-1 through transcription factor docking

Pere Puigserver, Guillaume Adelmant, Zhidan Wu, Melina Fan, Jianming Xu, Bert O'Malley, Bruce M. Spiegelman

Research output: Contribution to journal › Article › peer-review

468 Scopus citations

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 (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.

Original language	English (US)
Pages (from-to)	1368-1371
Number of pages	4
Journal	Science
Volume	286
Issue number	5443
DOIs	https://doi.org/10.1126/science.286.5443.1368
State	Published - Nov 12 1999
Externally published	Yes

ASJC Scopus subject areas

General

Access to Document

10.1126/science.286.5443.1368

Cite this

@article{4134ac1ca6a546caae4b583a03cc1a98,

title = "Activation of PPARγ coactivator-1 through transcription factor docking",

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 (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.",

author = "Pere Puigserver and Guillaume Adelmant and Zhidan Wu and Melina Fan and Jianming Xu and Bert O'Malley and Spiegelman, {Bruce M.}",

year = "1999",

month = nov,

day = "12",

doi = "10.1126/science.286.5443.1368",

language = "English (US)",

volume = "286",

pages = "1368--1371",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "5443",

}

TY - JOUR

T1 - Activation of PPARγ coactivator-1 through transcription factor docking

AU - Puigserver, Pere

AU - Adelmant, Guillaume

AU - Wu, Zhidan

AU - Fan, Melina

AU - Xu, Jianming

AU - O'Malley, Bert

AU - Spiegelman, Bruce M.

PY - 1999/11/12

Y1 - 1999/11/12

N2 - 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 (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.

AB - 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 (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.

UR - http://www.scopus.com/inward/record.url?scp=0032589689&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032589689&partnerID=8YFLogxK

U2 - 10.1126/science.286.5443.1368

DO - 10.1126/science.286.5443.1368

M3 - Article

C2 - 10558993

AN - SCOPUS:0032589689

SN - 0036-8075

VL - 286

SP - 1368

EP - 1371

JO - Science

JF - Science

IS - 5443

ER -

Activation of PPARγ coactivator-1 through transcription factor docking

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this