Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2022 May 9;18(8):3447-3457.
doi: 10.7150/ijbs.72244. eCollection 2022.

Emerging roles of protein palmitoylation and its modifying enzymes in cancer cell signal transduction and cancer therapy

Zhuang Liu  1 , Mingming Xiao  1 , Yaqi Mo  2 , Han Wang  1 , Yamei Han  1 , Xu Zhao  1 , Xue Yang  1 , Zhenxing Liu  2 , Bo Xu  1   2
Affiliations
Review

Emerging roles of protein palmitoylation and its modifying enzymes in cancer cell signal transduction and cancer therapy

Zhuang Liu et al. Int J Biol Sci. .

Abstract

Protein palmitoylation is an increasingly investigated form of post-translational lipid modification that affects protein localization, accumulation, secretion and function. Recently, emerging findings have revealed that protein palmitoylation is crucial for many tumor-related signaling pathways, such as EGFR, RAS, PD-1/PD-L1 signaling, affecting the occurrence, progression and therapeutic response of tumors. Protein palmitoylation and its modifying enzymes, including palmitoylases and depalmitoylases, are expected to be new targets for effective tumor treatment. Recognizing the significance of palmitoylation modification on protein stability, localization and downstream signal regulation, this review focuses on the regulatory roles of protein palmitoylation and its modifying enzymes in tumor cell signal transduction, aiming to bring new ideas for effective cancer prevention and treatment.

Keywords: DNA damage response; Depalmitoylase; Palmitoylase; Palmitoylation; Signal transduction.

PubMed Disclaimer

Conflict of interest statement

Competing Interests: The authors have declared that no competing interest exists.

Figures

Figure 1
Figure 1
Types of protein palmitoylation: S-palmitoylation, N-palmitoylation and O-palmitoylation.
Figure 2
Figure 2
The links of palmitoylases and depalmitoylases with cancer.
Figure 3
Figure 3
The role of protein palmitoylation in cancer cell signal transduction and tumor microenvironment.
See this image and copyright information in PMC

References

    1. Conradi C, Shiu A. Dynamics of Posttranslational Modification Systems: Recent Progress and Future Directions. Biophysical journal. 2018;114:507–15. - PMC - PubMed
    1. Jiang H, Zhang X, Chen X, Aramsangtienchai P, Tong Z, Lin H. Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies. Chemical reviews. 2018;118:919–88. - PMC - PubMed
    1. Wang Y, Yang W. Proteome-Scale Analysis of Protein S-Acylation Comes of Age. Journal of proteome research. 2021;20:14–26. - PMC - PubMed
    1. Resh MD. Palmitoylation of proteins in cancer. Biochemical Society transactions. 2017;45:409–16. - PubMed
    1. Malgapo MIP, Linder ME. Substrate recruitment by zDHHC protein acyltransferases. Open biology. 2021;11:210026. - PMC - PubMed

Publication types