Characterization of the effects and functions of sumoylation through rapamycin-mediated heterodimerization.
Post-translational modification of proteins, such as phosphorylation, ubiquitination, and SUMO modification, is an important means of regulating a variety of cellular activities. SUMOs (Small Ubiquitin related Modifiers) are covalently conjugated to lysine residues of many proteins by a mechanism that parallels ubiquitination (1). The effects of sumoylation, however, are distinct from ubiquitination. Sumoylation does not directly control protein stability, but regulates proteins through various mechanisms that include modulation of protein-protein interactions, protein-nucleic acid interactions, subcellular protein localization, and enzymatic activity (1-4). There are many examples, however, where the molecular bases for the effects of sumoylation on protein function and on cellular processes remain unclear. Here, we outline the use of an inducible and reversible sumoylation system, based on rapamycin heterodimerization, as a novel tool to characterize the functions of sumoylation in mammalian cells.
Zhu
Shanshan
S
Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA.
Matunis
Michael J
MJ
D000818:Animals; D019411:Clinical Laboratory Techniques; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding / Q000187:drug effects; D055503:Protein Multimerization / Q000187:drug effects* / Q000502:physiology; D011499:Protein Processing, Post-Translational / Q000187:drug effects / Q000502:physiology*; D020123:Sirolimus / Q000494:pharmacology*; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*
D025841:Small Ubiquitin-Related Modifier Proteins; D020123:Sirolimus