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J Biol Chem. 2016 Mar 25;291(13):6714-22. doi: 10.1074/jbc.R115.692020. Epub 2016 Feb 5.

Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300.

Author information

1
From the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037-1000 dyson@scripps.edu.
2
From the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037-1000 wright@scripps.edu.

Abstract

The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered partners, as a part of their ubiquitous role in facilitating transcription of genes. CBP and p300 contain a number of small structured domains that provide scaffolds for the interaction of disordered transactivation domains from a wide variety of partners, including p53, hypoxia-inducible factor 1α (HIF-1α), NF-κB, and STAT proteins, and are the targets for the interactions of disordered viral proteins that compete with cellular factors to disrupt signaling and subvert the cell cycle. The functional diversity of the CBP/p300 interactome provides an excellent example of the power of intrinsic disorder to facilitate the complexity of living systems.

KEYWORDS:

IDP; IDR; STAT transcription factor; cAMP response element-binding protein (CREB); coupled folding and binding; hypoxia-inducible factor (HIF); intrinsically disordered protein; intrinsically disordered region; protein-protein interaction; structure-function; transcriptional activation; transcriptional coactivator; viral oncoprotein

PMID:
26851278
PMCID:
PMC4807259
DOI:
10.1074/jbc.R115.692020
[Indexed for MEDLINE]
Free PMC Article

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