Simultaneous Measurement of SUMOylation using SNAP/CLIP-Tag-Mediated Translation at the Single-Molecule Level

摘要

SUMOylation, the covalent attachment of a SUMO monomer (SUMO = small ubiquitin-like modifier) or polySUMO chains to a target protein, regulates a variety of cellular processes. Perturbation of this modification system causes serious growth defects in yeast and embryonic lethality in mice. SUMOylation is also involved in the pathogenesis of several human diseases, including cancer, Parkinson's diseases, Huntington's disease, type 1 diabetes (T1D), and heart diseases. The molecular mechanism underlying these various effects and functions is the diversity of SUMOylation substrates within the cell. To date, more than 750 proteins have been identified as targets of SUMOylation. These targets include tumor suppressors, transcription factors/ cofactors, DNA repair proteins, signal transduction proteins, nuclear core complex, chromosome-organization proteins, telomere-binding proteins, cell cycle regulators, and viral proteins. Because of the large number of SUMOylation substrates and their vital roles in cells, systematic characterization of SUMOylation is imperative for a comprehensive understanding of SUMO-mediated post-translational modification.