Literature DB >> 26851278

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

H Jane Dyson1, Peter E Wright2.   

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.
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Entities:  

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

Mesh:

Substances:

Year:  2016        PMID: 26851278      PMCID: PMC4807259          DOI: 10.1074/jbc.R115.692020

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  100 in total

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