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Review
. 2022 May 2:13:865975.
doi: 10.3389/fimmu.2022.865975. eCollection 2022.

Lysine Acetylation/Deacetylation Modification of Immune-Related Molecules in Cancer Immunotherapy

Peng Ding  1   2 , Zhiqiang Ma  2 , Dong Liu  3 , Minghong Pan  1 , Huizi Li  4 , Yingtong Feng  1 , Yimeng Zhang  5 , Changjian Shao  1 , Menglong Jiang  6 , Di Lu  2 , Jing Han  5 , Jinliang Wang  2 , Xiaolong Yan  1
Affiliations
Review

Lysine Acetylation/Deacetylation Modification of Immune-Related Molecules in Cancer Immunotherapy

Peng Ding et al. Front Immunol. .

Abstract

As major post-translational modifications (PTMs), acetylation and deacetylation are significant factors in signal transmission and cellular metabolism, and are modulated by a dynamic process via two pivotal categories of enzymes, histone acetyltransferases (HATs) and histone deacetylases (HDACs). In previous studies, dysregulation of lysine acetylation and deacetylation has been reported to be associated with the genesis and development of malignancy. Scientists have recently explored acetylation/deacetylation patterns and prospective cancer therapy techniques, and the FDA has approved four HDAC inhibitors (HDACi) to be used in clinical treatment. In the present review, the most recent developments in the area of lysine acetylation/deacetylation alteration in cancer immunotherapy were investigated. Firstly, a brief explanation of the acetylation/deacetylation process and relevant indispensable enzymes that participate therein is provided. Subsequently, a multitude of specific immune-related molecules involved in the lysine acetylation/deacetylation process are listed in the context of cancer, in addition to several therapeutic strategies associated with lysine acetylation/deacetylation modification in cancer immunotherapy. Finally, a number of prospective research fields related to cancer immunotherapy concepts are offered with detailed analysis. Overall, the present review may provide a reference for researchers in the relevant field of study, with the aim of being instructive and meaningful to further research as well as the selection of potential targets and effective measures for future cancer immunotherapy strategies.

Keywords: Cancer; HAT; HDAC; acetylation; deacetylation; immunotherapy.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Lysine acetylation/deacetylation process that mediated by HATs and HDACs. HATs, histone acetyltransferases; HDACs, histone deacetylases; SIRTs, sirtuins.
Figure 2
Figure 2
Main acetylation/deacetylation-immunity relationships. Acetylation/deacetylation process can modulate immune activity and response via various ways, for instance, regulating the expression level of cytokines, regulating proliferation, infiltration and activity of immune cells, regulating the activity of immune cell receptors and regulating the expression and translocation of cell surface and cytosolic proteins, which causes immune activation or suppression in tumor microenvironment and thus influencing tumor development and progression.
Figure 3
Figure 3
Some cancer immunotherapeutic molecules and signaling pathways regulated by HATs. HATs, histone acetyltransferases; CBP, CREB-binding protein; OX40, tumor necrosis factor receptor superfamily member 4; CTLA-4, cytotoxic T-lymphocyte-associated antigen 4; PD-L1, programmed death-1 ligand; pSTAT1, phosphorylated STAT1; BRD4, bromodomain-containing 4.
Figure 4
Figure 4
Some cancer immunotherapeutic molecules and signaling pathways regulated by HDACs. HDACs, histone deacetylases; SIRTs, sirtuins; OX40, tumor necrosis factor receptor superfamily member 4; OX40L, OX40 ligand; 4-1BBL, 4-1BB ligand; RFX1, regulatory factor X 1; PD-L1, programmed death-1 ligand; STAT3, signal transducer and activator of transcription 3; COP1, constitutive photomorphogenesis protein 1; tim, TIM-3, T-cell immunoglobulin and mucin domain 3; LAG-3, lymphocyte-activation gene 3.
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