title: Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300.
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.
authors: From the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037-1000 dyson@scripps.edu.
authors: H Jane
authors: http://orcid.org/0000-0001-6855-3398
authors: HJ
authors: Dyson
authors: From the Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037-1000 wright@scripps.edu.
authors: Peter E
authors: http://orcid.org/0000-0002-1368-0223
authors: PE
authors: Wright
mesh_terms: D050882:CREB-Binding Protein / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D050881:E1A-Associated p300 Protein / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D051795:Hypoxia-Inducible Factor 1, alpha Subunit / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D016328:NF-kappa B / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D050791:STAT Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: C497442:HIF1A protein, human; D051795:Hypoxia-Inducible Factor 1, alpha Subunit; D064267:Intrinsically Disordered Proteins; D016328:NF-kappa B; D050791:STAT Transcription Factors; D016159:Tumor Suppressor Protein p53; D014764:Viral Proteins; D050882:CREB-Binding Protein; C494363:CREBBP protein, human; D050881:E1A-Associated p300 Protein; C494360:EP300 protein, human
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