Protein palmitoylation in cancer: molecular functions and therapeutic potential.
Protein palmitoylation in cancer: molecular functions and therapeutic potential.
复制标题
癌症中的蛋白质棕榈酰化:分子功能和治疗潜力。
DOI:
10.1002/1878-0261.13308
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发表时间:
2023-01
影响因子:
6.6
通讯作者:
Kong, Eryan
中科院分区:
文献类型:
--
作者:
Zhou, Binhui;Hao, Qianyun;Liang, Yinming;Kong, Eryan
Protein S‐palmitoylation (hereinafter referred to as protein palmitoylation) is a reversible lipid posttranslational modification catalyzed by the zinc finger DHHC‐type containing (ZDHHC) protein family. The reverse reaction, depalmitoylation, is catalyzed by palmitoyl‐protein thioesterases (PPTs), including acyl‐protein thioesterases (APT1/2), palmitoyl protein thioesterases (PPT1/2), or alpha/beta hydrolase domain‐containing protein 17A/B/C (ABHD17A/B/C). Proteins encoded by several oncogenes and tumor suppressors are modified by palmitoylation, which enhances the hydrophobicity of specific protein subdomains, and can confer changes in protein stability, membrane localization, protein–protein interaction, and signal transduction. The importance for protein palmitoylation in tumorigenesis has just started to be elucidated in the past decade; palmitoylation appears to affect key aspects of cancer, including cancer cell proliferation and survival, cell invasion and metastasis, and antitumor immunity. Here we review the current literature on protein palmitoylation in the various cancer types, and discuss the potential of targeting of palmitoylation enzymes or palmitoylated proteins for tumor treatment. Several oncogenes and tumor suppressors are modified by protein palmitoylation, a process that is dynamically controlled by the ZDHHC and PPT enzyme families, which add and remove palmitate, respectively. Palmitoylation affects protein stability, protein–protein interactions, membrane localization, and signaling transduction, thereby regulating tumor survival and tumor progression. Palmitoylation enzymes or palmitoylated proteins are potential targets for tumor treatment.
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