Protein ubiquitination plays important roles in plants, including stress responses. The
ubiquitin (Ub) E2 enzymes are required in the transfer of Ub to a substrate and are also …

Ubiquitination is mediated by an enzymatic cascade that results in the modification of
substrate proteins, redefining their fate. This post‐translational modification is involved in …

Background The ubiquitin 26S/proteasome system (UPS), a serial cascade process of
protein ubiquitination and degradation, is the last step for most cellular proteins. There are …

Ubiquitin is a highly conserved protein involved in several important regulatory processes
through its ATP-dependent, covalent ligation to a variety of eukaryotic target proteins. We …

Background Controlled turnover of proteins as mediated by the ubiquitin proteasome system
(UPS) is an important element in plant defense against environmental and pathogen …

The covalent attachment of the 76 amino acid protein ubiquitin is an important prerequisite
for the degradation of many eukaryotic proteins. The specificity of this ligation is …

The posttranslational addition of ubiquitin (Ub) profoundly controls the half-life, interactions,
and/or trafficking of numerous intracellular proteins. Using stringent two-step affinity methods …

Ubiquitin-conjugating enzymes (UBCs), which catalyse the transfer of ubiquitin to substrate
or E3 ligases, are key enzymes in ubiquitination modifications of target proteins. Current …

Summary Unlike conventional lysine (K) 48–linked polyubiquitination, K63‐linked
polyubiquitination plays signaling roles in yeast and animals. Thus far, UBC 13 is the only …

Selective modification of proteins by ubiquitination is directed by diverse families of ubiquitin-
protein ligases (or E3s). A large collection of E3s use Cullins (CULs) as scaffolds to form …