[Abstract]

Regulation of proteins via post-translational modification (PTM) by ubiquitin or ubiquitin-like proteins (ubiquitination, ISGylation, SUMOylation, or UFMylation) underlies a wide variety of cellular activities, involving protein stability, intracellular trafficking, the control of cell cycle, stress responses, signaling transduction, and immune modulation. Moreover, deregulation of these PTM systems gives rise to numerous human diseases, including cancers, neurodegenerative diseases, and immune diseases. Recent suggestion that targeting of these PTMs can be efficacious in the treatment of human cancers drives attempts to modulate the activities of components involved in post-translational protein modification pathways. Especially, understanding the mechanisms underlying tumor cell responsiveness to therapy might be expected to allow stratification of patients for personalized treatment. Here, I will present the intriguing roles of post-translational protein modifications not only in the pathogenesis of cancer but also in the response to therapies for cancer, which could contribute to therapeutic intervention in cancer.