The O-GlcNAc modification is a dynamic post-translational modification found on hundreds of mammalian proteins.  Despite the ubiquity of the O-GlcNAc modification, its roles in regulating the function and interactions of modified proteins remain poorly defined.  Recently, we developed a metabolic labeling method to selectively incorporate the diazirine photocrosslinker onto O-GlcNAc-modified proteins in a cellular setting.  Subsequent UV irradiation of the cells results in the formation of covalent crosslinks between O-GlcNAc-modified proteins and their neighbors.  We have validated our method by examining the interactions of phenylalanine-glycine (FG) repeat nucleoporins, a set of O-GlcNAc-modified proteins that line the nuclear pore.  We found that two of these FG-repeat nucleoporins, NUP153 and NUP358, crosslink to nuclear transport factors.  We report our current efforts in extending this study to another FG-repeat nucleoporin, NUP98 to determine the O-GlcNAc-dependent interactions in which it engages.

Exploration of O-GlcNAc-ylated protein interactions using a metabolically incorporated photo-crosslinking sugar

243rd National Meeting (2012)

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