Protein Lysine Acetylation by p300/CBP

Dancy, Beverley M.; Cole, Philip A.

doi:10.1021/cr500452k

Cited by 431 publications

(539 citation statements)

References 416 publications

(758 reference statements)

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“…Binding to TAZ2 also brings the transcription factor close to the HAT domain, providing an additional level of regulation through acetylation-mediated mechanisms (37).…”

Section: Taz2 Interactionsmentioning

confidence: 99%

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

Dyson

Wright

2016

Journal of Biological Chemistry

275

270

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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, hypoxiainducible factor 1␣ (HIF-1␣), NF-B, 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.

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“…Binding to TAZ2 also brings the transcription factor close to the HAT domain, providing an additional level of regulation through acetylation-mediated mechanisms (37).…”

Section: Taz2 Interactionsmentioning

confidence: 99%

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

Dyson

Wright

2016

Journal of Biological Chemistry

275

270

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“…In contrast, the SRCs serve as scaffold proteins to recruit additional coregulators (many of which possess protein-modifying activities) to ERα-binding sites, including p300/CBP (Dasgupta et al 2014;Yi et al 2015). The interactions of p300/CBP with ERα are mediated through the SRC proteins (Kim et al 2001;Dancy and Cole 2015;Yi et al 2015). p300/ CBP acetylates histones, TFs, and other coregulators and have also been used as a mark of active enhancers (Visel et al 2009;Dasgupta et al 2014;Dancy and Cole 2015).…”

mentioning

confidence: 99%

“…The interactions of p300/CBP with ERα are mediated through the SRC proteins (Kim et al 2001;Dancy and Cole 2015;Yi et al 2015). p300/ CBP acetylates histones, TFs, and other coregulators and have also been used as a mark of active enhancers (Visel et al 2009;Dasgupta et al 2014;Dancy and Cole 2015). Amplifications, mutations, and aberrant functions of Mediator, SRCs, and p300/CBP have been implicated in some types of cancers, including hormone-dependent cancers (Anzick et al 1997;Barbieri et al 2012;Dasgupta et al 2014).…”

mentioning

confidence: 99%

Dynamic assembly and activation of estrogen receptor α enhancers through coregulator switching

Murakami

Nagari

Kraus³

2017

Genes Dev.

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Although many features of active transcriptional enhancers have been defined by genomic assays, we lack a clear understanding of the order of events leading to enhancer formation and activation as well as the dynamics of coregulator interactions within the enhancer complex. Here, we used selective loss-or gain-of-function mutants of estrogen receptor α (ERα) to define two distinct phases of ligand-dependent enhancer formation. In the first phase (0-20 min), p300 is recruited to ERα by Mediator as well as p300's acetylhistone-binding bromodomain to promote initial enhancer formation, which is not competent for sustained activation. In the second phase (20-45 min), p300 is recruited to ERα by steroid receptor coregulators (SRCs) for enhancer maturation and maintenance. Successful transition between these two phases ("coregulator switching") is required for proper enhancer function. Failure to recruit p300 during either phase leads to abortive enhancer formation and a lack of target gene expression. Our results reveal an ordered and cooperative assembly of ERα enhancers requiring functional interplay among p300, Mediator, and SRCs, which has implications for hormone-dependent gene regulation in breast cancers. More broadly, our results demonstrate the unexpectedly dynamic nature of coregulator interactions within enhancer complexes, which are likely to be a defining feature of all enhancers.

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“…3), permitting a possible association through nuclear proteins. The transcriptional coactivator and histone acetyltransferase p300 is known to regulate chromatin conformation and DNA transcription (250). Concrete evidence suggests that p300 physically interacts with HIV-1 Tat (251-254) and integrase (255,256).…”

Section: Tat-p300/swi/snf-integrase Associationmentioning

confidence: 99%

HIV Genome-Wide Protein Associations: a Review of 30 Years of Research

Clercq

2016

Microbiol Mol Biol Rev

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SUMMARYThe HIV genome encodes a small number of viral proteins (i.e., 16), invariably establishing cooperative associations among HIV proteins and between HIV and host proteins, to invade host cells and hijack their internal machineries. As a known example, the HIV envelope glycoprotein GP120 is closely associated with GP41 for viral entry. From a genome-wide perspective, a hypothesis can be worked out to determine whether 16 HIV proteins could develop 120 possible pairwise associations either by physical interactions or by functional associations mediated via HIV or host molecules. Here, we present the first systematic review of experimental evidence on HIV genome-wide protein associations using a large body of publications accumulated over the past 3 decades. Of 120 possible pairwise associations between 16 HIV proteins, at least 34 physical interactions and 17 functional associations have been identified. To achieve efficient viral replication and infection, HIV protein associations play essential roles (e.g., cleavage, inhibition, and activation) during the HIV life cycle. In either a dispensable or an indispensable manner, each HIV protein collaborates with another viral protein to accomplish specific activities that precisely take place at the proper stages of the HIV life cycle. In addition, HIV genome-wide protein associations have an impact on anti-HIV inhibitors due to the extensive cross talk between drug-inhibited proteins and other HIV proteins. Overall, this study presents for the first time a comprehensive overview of HIV genome-wide protein associations, highlighting meticulous collaborations between all viral proteins during the HIV life cycle.

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Protein Lysine Acetylation by p300/CBP

Cited by 431 publications

References 416 publications

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

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

Dynamic assembly and activation of estrogen receptor α enhancers through coregulator switching

HIV Genome-Wide Protein Associations: a Review of 30 Years of Research

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