Protein S-palmitoylation modification: implications in tumor and tumor immune microenvironment

Front Immunol. 2024 Feb 13:15:1337478. doi: 10.3389/fimmu.2024.1337478. eCollection 2024.

Abstract

Protein S-palmitoylation is a reversible post-translational lipid modification that involves the addition of a 16-carbon palmitoyl group to a protein cysteine residue via a thioester linkage. This modification plays a crucial role in the regulation protein localization, accumulation, secretion, stability, and function. Dysregulation of protein S-palmitoylation can disrupt cellular pathways and contribute to the development of various diseases, particularly cancers. Aberrant S-palmitoylation has been extensively studied and proven to be involved in tumor initiation and growth, metastasis, and apoptosis. In addition, emerging evidence suggests that protein S-palmitoylation may also have a potential role in immune modulation. Therefore, a comprehensive understanding of the regulatory mechanisms of S-palmitoylation in tumor cells and the tumor immune microenvironment is essential to improve our understanding of this process. In this review, we summarize the recent progress of S-palmitoylation in tumors and the tumor immune microenvironment, focusing on the S-palmitoylation modification of various proteins. Furthermore, we propose new ideas for immunotherapeutic strategies through S-palmitoylation intervention.

Keywords: immunotherapeutic strategies; lipid modification; protein S-palmitoylation; tumor cells; tumor immune microenvironment.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cysteine
  • Humans
  • Lipoylation*
  • Neoplasms*
  • Protein Processing, Post-Translational
  • Tumor Microenvironment

Substances

  • Cysteine

Grants and funding

The author(s) declare financial support was received for the research, authorship, and/or publication of this article. This work was supported by the Major International (Regional) Joint Research Program of the National Natural Science Foundation of China (No. 81920108027), National Natural Science Foundation of China (No. 82271885), and Natural Science Foundation of Chongqing (No. cstc2021jcyj-msxmX0111).