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Coactivator recruitment: a new role for PAS domains in transcriptional regulation by the bHLH-PAS family.

Authors
  • Partch, Carrie L
  • Gardner, Kevin H
Type
Published Article
Journal
Journal of Cellular Physiology
Publisher
Wiley
Publication Date
Jun 01, 2010
Volume
223
Issue
3
Pages
553–557
Identifiers
DOI: 10.1002/jcp.22067
PMID: 20112293
Source
Medline
License
Unknown

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.

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