Advances in post-translational modifications of proteins and cancer immunotherapy
Protein post-translational modification (PTM) is a regulatory mechanism for protein activity modulation, localization, expression, and interactions with other cellular molecules. It involves the addition or removal of specific chemical groups on the amino acid residues of proteins. Its common forms...
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Published in: | Frontiers in immunology Vol. 14; p. 1229397 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
Frontiers Media S.A
22-08-2023
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Subjects: | |
Online Access: | Get full text |
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Summary: | Protein post-translational modification (PTM) is a regulatory mechanism for protein activity modulation, localization, expression, and interactions with other cellular molecules. It involves the addition or removal of specific chemical groups on the amino acid residues of proteins. Its common forms include phosphorylation, ubiquitylation, methylation, and acetylation. Emerging research has highlighted lactylation, succinylation, and glycosylation. PTMs are involved in vital biological processes. The occurrence and development of diseases depends on protein abundance and is regulated by various PTMs. In addition, advancements in tumor immunotherapy have revealed that protein PTM is also involved in the proliferation, activation, and metabolic reprogramming of immune cells in tumor microenvironment. These PTMs play an important role in tumor immunotherapy. In this review, we comprehensively summarize the role of several types of PTMs in tumor immunotherapy. This review could provide new insights and future research directions for tumor immunotherapy. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 These authors share first authorship Edited by: Xiangpeng Dai, Jilin University, China Reviewed by: Kai Xu, Huazhong University of Science and Technology, China; Wei Su, The First Affiliated Hospital of Xinxiang Medical University, China; Jia Liu, Qingdao University, China |
ISSN: | 1664-3224 1664-3224 |
DOI: | 10.3389/fimmu.2023.1229397 |