Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Cell Physiol. 2010 Jun;223(3):553-7. doi: 10.1002/jcp.22067.

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

Author information

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-8816, USA.

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.

(c) 2010 Wiley-Liss, Inc.

PMID:
20112293
[PubMed - indexed for MEDLINE]
PMCID:
PMC2872778
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for John Wiley & Sons, Inc. Icon for PubMed Central
    Loading ...
    Write to the Help Desk