Protein modification systems as cancer biomarkers and therapeutic targets

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Authors: Li Gao, Yulong He, K Wang, Qi Li, Litong Nie, Lunzhi Dai
Cited by: 1
References: 295

Abstract

Protein post-translational modifications (PTMs), such as acetylation, lactylation, methylation, phosphorylation, ubiquitination, and glycosylation, play central roles in regulating diverse cellular processes, including signal transduction, metabolic adaptation, chromatin organization, and proteostasis. In cancer, PTM networks are extensively rewired, with profound alterations in enzyme levels, protein modification landscapes, and crosstalk among different modification types. These changes collectively shape key cancer hallmarks, such as sustained proliferative signaling, immune evasion, and therapeutic resistance. Recent advances in proteomic technologies have enabled comprehensive mapping of PTM landscapes and their regulatory mechanisms, facilitating the identification of PTM signatures associated with tumor subtyping, disease progression, and treatment response. This review summarized biomarkers and therapeutic targets associated with dysregulated PTM regulatory pathways in cancer.

Fields of Study & Subjects

Peptidase Inhibition and Analysis Protein Degradation and Inhibitors Cancer-related gene regulation

Publication details

Journal / source
Precision Clinical Medicine
Publisher
Oxford University Press (OUP)
Volume
9
Issue
2
Pages
pbag014–pbag014
Publication date
11 April 2026
Language
EN