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Editorial
. 2016 Dec 6;7(49):80101-80102.
doi: 10.18632/oncotarget.12989.

Acidic domains: "converse readers" for acetylation code

Donglai Wang, Ning Kon, Wei Gu
Editorial

Acidic domains: "converse readers" for acetylation code

Donglai Wang et al. Oncotarget. .
No abstract available

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Figures

Figure 1
Figure 1. Schematic diagram of C-terminal domain (CTD) acetylation-mediated regulation of p53- dependent transcription
In unstressed conditions, unacetylated p53 recruits various acidic domain (AD)- containing proteins (e.g. SET, VPRBP, DAXX and PELP1) due to the charge effect between the p53 CTD and the acidic domain of these proteins. Upon stresses (e.g. DNA damage), the p53 CTD acetylation is highly induced, which in turn neutralizes the positive charge of the CTD and abolishes p53 interactions with these AD-containing proteins. AD-containing proteins, in a separate or a combined manner, modulate p53 in multiple aspects (e.g. stability, DNA-binding affinity), which may contribute to gene-specific transcription of p53 downstream targets.
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