Ubiquitin Peptides

Ubiquitylation is a post-translational modification involving the covalent binding of the small, highly conserved protein ubiquitin to a target substrate to regulate protein functions. The ligation of the ubiquitin C-terminus to a target protein is facilitated by a cascade of ubiquitin-activating and ligating enzymes and reversed by deubiquitylating enzymes (DUBs). Ubiquitin possesses seven lysine residues and an N-terminus (M1, K6, K11, K29, K33, K48 and K63), any one of which can be ubiquitylated itself leading to the assembly of polyubiquitin chains. Any of these chains lead to different biological outcomes. For example, while K48 chains lead to proteasomal degradation, K63 chains are linked to cell signalling trafficking and lysosomal degradation.

Ubiquitin signalling is integral to almost all cellular processes in eukaryotes and thus, disorders or mutations in ubiquitin pathways often result in diseases including cancer, a wide range of autoimmune diseases as well as neurodegenerative diseases such as Parkinson’s, Alzheimer’s and Huntington’s disease.

Mass spectrometry (MS)-based proteomics has become a powerful method for the analysis of ubiquitylation in the last 15 years. Particularly, targeted MS approaches using heavy isotope labelled K-GG peptides help to identify and quantify ubiquitin chain topologies.

Heap, R.E., Gant, M.S., Lamoliatte, F., Peltier, J. and Trost, M., Mass spectrometry techniques for studying the ubiquitin system (2017), Biochem Soc Transactions, Oct 15;45(5):1137-1148.

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