β-arrestins recruit Nedd4 ubiquitin E3 ligase to mGlu7 receptor and facilitate ubiquitination, endocytosis, ERK signaling, and stability of mGlu7 at presynaptic terminals.
Yersinia pseudotuberculosis and enteropathogenic Escherichia coli promote pathogenicity by deamidating the ubiquitin-like protein NEDD8 to block ubiquitin-dependent trafficking of Perforin-2, which is an effector of innate immunity.
Structural studies reveal the mechanism by which a HECT E3 ubiquitin ligase carries out E2-to-E3-to-substrate ubiquitin transfer and prioritizes target lysines for ubiquitination.
The general principles that underlie the mechanism of action of the COP9-Signalosome, a key regulator of the largest family of ubiquitin ligase enzymes in human cells, have been identified using structural and kinetic techniques.
A novel engineered protein that uncouples electrical signals from downstream biological responses in excitable cells provides a unique investigative tool with potential therapeutic applications.
A protein interaction screen revealed desmosomes as a scaffold for the COP9 de-neddylating complex, to promote epidermal differentiation by governing the balance of Nedd8 and Ubiquitin modifications on Epidermal Growth Factor Receptor.
Simultaneous phosphorylation of multiple substrate motifs drives switch-like target recognition and monoubiquitylation by an E3 ligase during metazoan development.
