Succinylation in cancer immunotherapy: mechanisms, biomarkers, and therapeutic implications

Succinylation, a dynamic post-translational modification characterized by the addition of a succinyl moiety to lysine residues, has emerged as a pivotal regulator at the interface of metabolic reprogramming and immune surveillance in cancer. This review systematically delineates the molecular mechanisms and therapeutic implications of succinylation in cancer immunotherapy. We detail the writers (e.g., CPT1A, KAT2A), erasers (e.g., SIRT5, SIRT7), and readers that constitute the enzymatic systems