Succinylation in lung cancer: mechanisms, implications, and clinical perspectives

As a form of protein posttranslational modification (PTM), succinylation involves the covalent addition of a succinyl moiety to specific residues (predominantly lysine) in proteins through an amide linkage, altering protein activity, stability, and intermolecular interactions. By influencing these molecular properties, succinylation contributes substantially to the control of cellular metabolism, intracellular signaling, and transcriptional regulation. Accumulating evidence suggests that abnormal succinylation is implicated in both the onset and progression of lung cancer. This review provides a systematic overview of the molecular processes through which succinylation participates in lung tumorigenesis and evaluates prospective treatment approaches and future directions with a focus on succinylation as a therapeutic target. Taken together, the available evidence supports further investigation of the biological relevance of succinylation to lung tumor biology and may promote the development and eventual clinical translation of therapies directed against succinylation-related pathways.