Post-translational modifications of high mobility group box 1 and cancer.

Post-translational modifications (PTMs) of High mobility group box 1 (HMGB1) have not been investigated as extensively as those of other HMG proteins but accumulating evidence has shown the remarkable biological significances induced by the post-translational: acetylation, methylation and phosphorylation, oxidation, glycosylation and ADP-ribosylation of the HMGB1 to modulate its interactions with DNA and other proteins. Although HMGB1 is localized in the nucleus in almost all cells at baseline, it can be rapidly mobilized to other sites within the cell, including the cytoplasm and mitochondria, as well as into the extracellular; hence there is an increasing interest by researches into the complex relationship between the PTMs of HMGB1 protein and its diverse biological activities. The PTMs of HMGB1 could also have effects on gene expression following changes in its DNA-binding properties and in extracellular environment displays immunological activity and could serve as a potential target for new therapy. Our reviewed identifies covalent modifications of HMGB1, and highlighted how these PTMs affect the functions of HMGB1 protein in a variety of cellular and extra cellular processes as well as diseases and therapy.