Abstract
Publisher Summary The covalent modification of target proteins by the polypeptide ubiquitin (Ub) is involved in a wide array of cellular processes, ranging from cell cycle progression and receptor-mediated endocytosis to endoplasmic reticulum-associated degradation and cell-type specification. The best understood function of ubiquitination is to tag protein substrates for destruction, with a polymeric chain of Ub molecules being required to target the substrate to the 26S proteasome for hydrolysis. In addition to this common role in protein degradation, a number of examples of nonproteolytic functions for Ub attachment also exist. This chapter describes various methods to determine whether Ub modifies a particular protein in vivo. These assays can be adapted to ask if the substrate is attached to Ub chains and to ascertain the topology (linkages) of the Ub monomers in these polymeric chains. The chapter also discusses the methods for determining the enzymes that are required for substrate ubiquitination.
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