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 …

Cullin-based E3 ubiquitin ligases play important roles in the regulation of diverse
developmental processes and environmental responses in eukaryotic organisms. Recently …

Selective ubiquitination of proteins is directed by diverse families of ubiquitin-protein ligases
(or E3s) in plants. One important type uses Cullin-3 as a scaffold to assemble multisubunit …

Cullin proteins, which belong to multigenic families in all eukaryotes, associate with other
proteins to form ubiquitin protein ligases (E3s) that target substrates for proteolysis by the …

Thirty years of research have revealed the fundamental role of the ubiquitin–proteasome
system in diverse aspects of cellular regulation in eukaryotes. The ubiquitin–protein ligases …

The posttranslational addition of ubiquitin (Ub) helps control the half-life, localization, and
action of many intracellular plant proteins. A primary function is the degradation of …

The ubiquitin proteasome pathway in plants has been shown to be important for many
developmental processes. The E3 ubiquitin-protein ligases facilitate transfer of the ubiquitin …

The ubiquitin/26S proteasome pathway largely mediates selective proteolysis in the nucleus
and cytosol. This pathway catalyzes covalent attachment of ubiquitin (UBQ) to substrate …

Due to their sessile nature, plants depend on flexible regulatory systems that allow them to
adequately regulate developmental and physiological processes in context with …

The past decade has witnessed an explosion in the identification of ubiquitin-ligase
complexes as the missing receptors for important small-molecule hormones regulating plant …