Post-translational modification pathways

Post-translational modification pathways" is not a single molecule or receptor, but rather a collective term for the diverse covalent modifications proteins undergo after biosynthesis. These modifications include phosphorylation, glycosylation, acetylation, ubiquitination, methylation, lipidation, and proteolytic cleavage, among others. PTMs regulate nearly every aspect of protein function—including their activity, localization, interactions, and stability—thereby influencing a vast array of cellular processes like signal transduction, cell cycle progression, immune response, apoptosis, and metabolism[1][3][4][5]. Abnormalities in PTM pathways are implicated in numerous diseases, such as cancer, neurodegenerative disorders, cardiovascular diseases, and inflammatory and metabolic conditions[1][3][6]. While individual PTM enzymes (for example, kinases, phosphatases, acetyltransferases) can be therapeutic targets, the term "post-translational modification pathways" denotes a process network, not a defined therapeutic target or single protein[1][3][6][7]. Critical clarification: "Post-translational modification pathways" should not be treated as a specific molecule or canonical drug target. It is a biological concept encompassing many molecular targets and mechanisms[1][3][9].

Other names

PTMPost-translational modificationsProtein post-translational modifications