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EDITORIAL article

Front. Immunol.
Sec. Cancer Immunity and Immunotherapy
Volume 15 - 2024 | doi: 10.3389/fimmu.2024.1533926
This article is part of the Research Topic Community Series in Post-Translational Modifications of Proteins in Cancer Immunity and Immunotherapy, Volume III View all 8 articles

Editorial: Community Series in Post-Translational Modifications of Proteins in Cancer Immunity and Immunotherapy, Volume III

Provisionally accepted
Xuejing Zhao Xuejing Zhao 1,2Naoe Taira Nihira Naoe Taira Nihira 3Xiangpeng Dai Xiangpeng Dai 4,5*Zichuan Liu Zichuan Liu 1,6*
  • 1 School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China
  • 2 Tianjin University and Health-Biotech United Group Joint Laboratory of Innovative Drug Development and Translational Medicine, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China
  • 3 Department of Translational Oncology, St. Marianna University Graduate School of Medicine,, Kawasaki, Japan
  • 4 Key Laboratory of Organ Regeneration and Transplantation of Ministry of Education, First Hospital of Jilin University,, Changchun, China
  • 5 National-Local Joint Engineering Laboratory of Animal Models for Human Disease, First Hospital of Jilin University, Changchun, China., Changchun, China
  • 6 Frontiers Science Center for Synthetic Biology (Ministry of Education), Tianjin University, Tianjin, China

The final, formatted version of the article will be published soon.

    Currently, more than 800 proteins with E3 enzyme activity have been identified In recent years, the UFMylation, a protein posttranslational modification similar to ubiquitination, has been found to regulate various cellular processes. UFMylation T lymphocytes, integral to the adaptive immune system, wield pivotal influence in bolstering anti-tumor responses, and are strictly regulated by ubiquitination modification. Chen et al. developed a novel riskscore based on the close interaction between T cells and ubiquitination modification. In this study, they identified 5 core T cell marker genes, including UBE2E1, PSMD1, FBXL5, IVNS1ABP, and RNF10 via bioinformatic analysis. PSMD1 can affect HCC cell proliferation and apoptosis by influencing lipid droplet formation (5). FBXL5 can prevent iron overload and inhibit HCC occurrence (6), and inhibit HCC by suppressing snail expression levels. RNF10 has been confirmed to be a core gene predicting the prognosis of HCC patients, so the study focused on UBE2E1 and demonstrated its carcinogenic effect in HCC through a series of in vitro cell experiments. The E3 ligase and other proteins with PTM function reveal potential mechanisms for tumor therapy, and it can also accurately predict the prognosis of patients with a certain type of cancer, which make it to be used as a decision-making tool to guide therapy. Intensive study of these related modifications and their regulatory mechanisms can help develop new cancer therapeutic strategies.

    Keywords: Protein post-translational modification (PTM), Ubiquitination, E3 ligase, Immunotherapy, Cancer

    Received: 25 Nov 2024; Accepted: 29 Nov 2024.

    Copyright: © 2024 Zhao, Nihira, Dai and Liu. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence:
    Xiangpeng Dai, Key Laboratory of Organ Regeneration and Transplantation of Ministry of Education, First Hospital of Jilin University,, Changchun, China
    Zichuan Liu, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, 300072, China

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