Most proteins of a cell become posttranslationally modified, either transiently or permanently. Substoichiometric modifications with a high turnover rate, like phosphorylation or N-acetylglucosaminylation of nucleocytosolic proteins play important roles in the regulation of protein function. Other modifications, like N,O-glycosylation or S-palmitoylation, were shown to be functionally involved in secretion or in the apical sorting and recycling of plasmamembrane proteins. A proteomics platform combining LC-MS and GC-MS technologies allows for the detection, the site localization and the structural characterization of most protein modifications described so far, including SUMOylation and ubiquitination. A workshop will provide insight into and training of MS/MS-based phosphopeptide and glycopeptide analysis in Arabidopsis including data management.

For a program schedule and detailed information on the workshop, please download the Acrobat Reader file attached below.