Coactivator recruitment

A new role for PAS domains in transcriptional regulation by the bHLH-PAS family

Carrie L. Partch, Kevin H. Gardner

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Transcriptional regulation is dependent on layers of interactions between transcription factors and coactivators, controlling the specificity, temporal regulation, and extent to which transcriptional programs are executed. A key issue in the field of transcriptional regulation is to identify structural mechanisms by which transcription factors and coactivators build hierarchical protein assemblies. The basic helix-loop-helix Per-ARNT-Sim domain (bHLH-PAS) family of transcriptional regulators comprises both transcription factors and coactivators, which have different functions despite conserved domain architecture. Within this family, the tandem PAS domains typically mediate dimerization of the transcription factors, while C-terminal transactivation domains facilitate the dynamic interplay between transcription factors and coactivators. However, recent studies have shown that the modular PAS domains play an important role in regulating coactivator recruitment and oligomerization status. In this study, we provide a brief overview of the structural and functional studies that have identified a novel protein interaction interface on PAS domains utilized by both transcription factors and coactivators within the bHLH-PAS family.

Original languageEnglish (US)
Pages (from-to)553-557
Number of pages5
JournalJournal of Cellular Physiology
Volume223
Issue number3
DOIs
StatePublished - Jun 2010

Fingerprint

Transcription Factors
Oligomerization
Dimerization
Transcriptional Activation
Proteins

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

Cite this

Coactivator recruitment : A new role for PAS domains in transcriptional regulation by the bHLH-PAS family. / Partch, Carrie L.; Gardner, Kevin H.

In: Journal of Cellular Physiology, Vol. 223, No. 3, 06.2010, p. 553-557.

Research output: Contribution to journalArticle

@article{583c210256454966b75c264e3e248826,
title = "Coactivator recruitment: A new role for PAS domains in transcriptional regulation by the bHLH-PAS family",
abstract = "Transcriptional regulation is dependent on layers of interactions between transcription factors and coactivators, controlling the specificity, temporal regulation, and extent to which transcriptional programs are executed. A key issue in the field of transcriptional regulation is to identify structural mechanisms by which transcription factors and coactivators build hierarchical protein assemblies. The basic helix-loop-helix Per-ARNT-Sim domain (bHLH-PAS) family of transcriptional regulators comprises both transcription factors and coactivators, which have different functions despite conserved domain architecture. Within this family, the tandem PAS domains typically mediate dimerization of the transcription factors, while C-terminal transactivation domains facilitate the dynamic interplay between transcription factors and coactivators. However, recent studies have shown that the modular PAS domains play an important role in regulating coactivator recruitment and oligomerization status. In this study, we provide a brief overview of the structural and functional studies that have identified a novel protein interaction interface on PAS domains utilized by both transcription factors and coactivators within the bHLH-PAS family.",
author = "Partch, {Carrie L.} and Gardner, {Kevin H.}",
year = "2010",
month = "6",
doi = "10.1002/jcp.22067",
language = "English (US)",
volume = "223",
pages = "553--557",
journal = "Journal of Cellular Physiology",
issn = "0021-9541",
publisher = "Wiley-Liss Inc.",
number = "3",

}

TY - JOUR

T1 - Coactivator recruitment

T2 - A new role for PAS domains in transcriptional regulation by the bHLH-PAS family

AU - Partch, Carrie L.

AU - Gardner, Kevin H.

PY - 2010/6

Y1 - 2010/6

N2 - Transcriptional regulation is dependent on layers of interactions between transcription factors and coactivators, controlling the specificity, temporal regulation, and extent to which transcriptional programs are executed. A key issue in the field of transcriptional regulation is to identify structural mechanisms by which transcription factors and coactivators build hierarchical protein assemblies. The basic helix-loop-helix Per-ARNT-Sim domain (bHLH-PAS) family of transcriptional regulators comprises both transcription factors and coactivators, which have different functions despite conserved domain architecture. Within this family, the tandem PAS domains typically mediate dimerization of the transcription factors, while C-terminal transactivation domains facilitate the dynamic interplay between transcription factors and coactivators. However, recent studies have shown that the modular PAS domains play an important role in regulating coactivator recruitment and oligomerization status. In this study, we provide a brief overview of the structural and functional studies that have identified a novel protein interaction interface on PAS domains utilized by both transcription factors and coactivators within the bHLH-PAS family.

AB - Transcriptional regulation is dependent on layers of interactions between transcription factors and coactivators, controlling the specificity, temporal regulation, and extent to which transcriptional programs are executed. A key issue in the field of transcriptional regulation is to identify structural mechanisms by which transcription factors and coactivators build hierarchical protein assemblies. The basic helix-loop-helix Per-ARNT-Sim domain (bHLH-PAS) family of transcriptional regulators comprises both transcription factors and coactivators, which have different functions despite conserved domain architecture. Within this family, the tandem PAS domains typically mediate dimerization of the transcription factors, while C-terminal transactivation domains facilitate the dynamic interplay between transcription factors and coactivators. However, recent studies have shown that the modular PAS domains play an important role in regulating coactivator recruitment and oligomerization status. In this study, we provide a brief overview of the structural and functional studies that have identified a novel protein interaction interface on PAS domains utilized by both transcription factors and coactivators within the bHLH-PAS family.

UR - http://www.scopus.com/inward/record.url?scp=77951220423&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77951220423&partnerID=8YFLogxK

U2 - 10.1002/jcp.22067

DO - 10.1002/jcp.22067

M3 - Article

VL - 223

SP - 553

EP - 557

JO - Journal of Cellular Physiology

JF - Journal of Cellular Physiology

SN - 0021-9541

IS - 3

ER -