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Front. Biol.    2018, Vol. 13 Issue (3) : 168-179    https://doi.org/10.1007/s11515-018-1502-6
REVIEW
CBP/p300: intramolecular and intermolecular regulations
Yongming Xue1,2(), Hong Wen1,3, Xiaobing Shi1,2,3()
1. Department of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, TX, 77030, USA
2. Genetics and Epigenetics Graduate Program, The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences, Houston, TX, 77030, USA
3. Center for Epigenetics, Van Andel Research Institute, Grand Rapids, MI, 49503, USA
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Abstract

BACKGROUND: CREB binding protein (CBP) and its close paralogue p300 are transcriptional coactivators with intrinsic acetyltransferase activity. Both CBP/p300 play critical roles in development and diseases. The enzymatic and biological functions of CBP/p300 are tightly regulated by themselves and by external factors. However, a comprehensive up-to-date review of the intramolecular and intermolecular regulations is lacking.

OBJECTIVE: To summarize the molecular mechanisms regulating CBP/p300s functions.

METHODS: A systematic literature search was conducted using the PubMed (https://www.ncbi.nlm.nih.gov/pubmed/) for literatures published during 1985-2018. Keywords “CBP regulation” or “p300 regulation” were used for the search.

RESULTS: The functions of CBP/p300, especially their acetyltransferase activity and chromatin association, are regulated both intramolecularly by their autoinhibitory loop (AIL), bromodomain, and PHD-RING region and intermolecularly by their interacting partners. The intramolecular mechanisms equip CBP/p300 with the capability of self-regulation while the intermolecular mechanisms allow them to respond to various cell signaling pathways.

CONCLUSION: Investigations into those regulation mechanisms are crucial to our understanding of CBP/p300s role in development and pathogenesis. Pharmacological interventions targeting these regulatory mechanisms have therapeutic potentials.
Keywords p300      CBP      histone acetylation      autoacetylation      HAT     
Corresponding Author(s): Yongming Xue,Xiaobing Shi   
Online First Date: 05 July 2018    Issue Date: 31 July 2018
 Cite this article:   
Yongming Xue,Hong Wen,Xiaobing Shi. CBP/p300: intramolecular and intermolecular regulations[J]. Front. Biol., 2018, 13(3): 168-179.
 URL:  
https://academic.hep.com.cn/fib/EN/10.1007/s11515-018-1502-6
https://academic.hep.com.cn/fib/EN/Y2018/V13/I3/168
Fig.1  Regulation of CBP/p300 acetyltransferase activity by AIL, RING domain and BRD. (A) Schematic representation of human CBP/p300 domain architecture. The numbers of residues are also labeled. (B) The HAT domain is in inactive state because hypoacetylated AIL occupies the substrate binding groove and also because RING domain is packed in close proximity to the HAT active site. CBP/p300 AIL can be autoacetylated in trans. HAT domain will become activated when RING domain and the hyperacetylated AIL are displaced from the catalytic site. (C) CBP/p300 BRD is a reader domain preferentially binds acetylated histone H4. The recognition of acetylated histone tail by BRD not only directly recruits CBP/p300 to chromatin but also increases the accessibility of histone substrate, for example, H3, to HAT domain, thus enhancing histone acetylation. Both in cis and in trans models are shown.
Fig.2  Summary of intramolecular and intermolecular mechanisms regulating CBP/p300 acetyltransferase activity (A) and chromatin association (B). Lines with arrows indicate positive regulation whereas blunt-ended lines indicate negative regulation. *: the negative regulatory role of RING domain in CBP/p300 acetyltransferase activity is specific to non-histone substrate.
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