Identification of SUMOylated and Ubiquitylated Substrates by Mass Spectrometry
Francis P. McManus and Pierre Thibault
from: SUMOylation and Ubiquitination: Current and Emerging Concepts (Edited by: Van G. Wilson). Caister Academic Press, U.K. (2019) Pages: 71-94.
Abstract
Further understanding of the cross-talk taking place between protein SUMOylation and ubiquitylation can provide valuable insights into the biological function and turnover of proteins. Recent advances in sample preparation and the development of sensitive mass spectrometers enabled a systems-level view of this cross communication. Here, we highlight the evolution as well as the merits and limitations of the various workflows that have been created to monitor protein SUMOylation and ubiquitylation. Furthermore, this chapter delves into mass spectrometry centered approaches to study the co-occurrence of SUMOylation and ubiquitylation on proteins in a non-biased large-scale fashion using immunoaffinity enrichment that target either the co-modified proteins from cell extracts or the modified peptides of the corresponding proteins. Lastly, we provide a perspective on methods that will permit the global analysis of endogenous proteins modified by different ubiquitin-like proteins (UBLs) read more ...
