Post-translational modifications act as rheostats of protein activity. Many them reflect environmental variations and allow the cell to give an adapted response these changes. In this cover article #Ref, Céline Schulz collaborators provide in-depth overview still underrated role nutrient-dependent post-translational modification O-GlcNAcylation in regulation metabolism lipids, a very heterogeno...

Post-translational modifications, such as acetylation and ubiquitination, can greatly expand the functionality of a particular protein. The promyelocytic leukemia (PML) protein is a functionally promiscuous protein with proposed roles in many cellular processes. Its cellular headquarters are the macromolecular structures termed PML nuclear bodies. Post-translational modification of PML is emerg...

Plasma proteins represent an important part of the human proteome. Although recent proteomics research efforts focus largely on determining the overall number of proteins circulating in plasma, it is equally important to delineate protein variations among individuals, because they can signal the onset of diseases and be used as biological markers in diagnostics. To date, there has been no syste...

BACKGROUND Minimotifs are short contiguous peptide sequences in proteins that have known functions. At its simplest level, the minimotif sequence is present in a source protein and has an activity relationship with a target, most of which are proteins. While many scientists routinely investigate new minimotif functions in proteins, the major web-based discovery tools have a high rate of false-p...

Posttranslational modification of proteins is important for signal transduction, and hence significant effort has gone toward understanding how posttranslational modification networks process information. This involves, on the theory side, analyzing the dynamical systems arising from such networks. Which networks are, for instance, bistable? Which networks admit sustained oscillations? Which pa...

SUMOylation, a reversible process used as a 'fine-tuning' mechanism to regulate the role of multiple proteins, is conserved throughout evolution. This post-translational modification affects several cellular processes by the modulation of subcellular localization, activity or stability of a variety of substrates. A growing number of proteins have been identified as targets for SUMOylation, alth...

Strategies for the chemical construction of synthetic proteins with precisely positioned post-translational modifications or their mimics offer a powerful method for dissecting the complexity of functional protein alteration and the associated complexity of proteomes.

Multi-site phosphorylation systems are repeatedly encountered in cellular biology and multi-site modification is a basic building block of post-translational modification. In this paper, we demonstrate how distributive multi-site modification mechanisms by a single kinase/phosphatase pair can lead to biphasic/partial biphasic dose-response characteristics for the maximally phosphorylated substr...

Results from ion mobility studies of tryptic peptides suggest that, in some cases, the gas-phase structures can be related to the solution-phase structure of the parent protein. The interpretation of ion mobility measurements is supported by results from molecular modeling and H/D exchange experiments on the same peptides. This study clearly illustrates the utility of IM-MS for screening comple...