The F-box and U-box E3 ubiquitin ligase decoy library is a powerful tool for the functional characterization of redundant E3 ubiquitin ligases, like MAC3A and MAC3B, novel circadian clock regulators.
E3 ubiquitin ligase Bre1-induced H2B monoubiquitination is epigenetically important for recruiting replication factor Mcm10 and cohesion establishment factors Ctf4, Ctf18 and Eco1 to early replication origins to establish sister chromatid cohesion.
CRISPR/Cas9 genome-wide screens using sterol-sensitive endogenous HMG-CoA reductase (HMGCR) reporter identify the sterol-responsive RNF145 and gp78 as independently responsible for sterol-accelerated degradation of HMGCR, the rate-limiting enzyme of cholesterol biosynthesis.
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.
Engineered E3 ubiquitin ligases are utilized to elucidate mechanisms underlying ubiquitin regulation of membrane proteins, and to achieve robust post-translational functional knockdown of ion channels.
Control of lipoprotein receptor protein levels at synapses by the E3 ubiquitin ligase IDOL is shown to be important for the plasticity of neuronal dendrites in vitro and learning and memory in mice.
RNF213 is a giant E3 ligase with a dynein-like core and a unique ubiquitination mechanism that proceeds in a RING-independent manner and is linked with the Moyamoya disease.
A cell-free system combined with cell-based assays elucidate the biochemical mechanism of signal transduction mediated by the mitochondrial protein MAVS and delineates the role of ubiquitin E3 ligases in antiviral innate immune responses.
The endoplasmic reticulum E3 ubiquitin ligase Doa10 and the mitochondrial AAA-ATPase Msp1 govern targeting fidelity of outer mitochondrial tail-anchored proteins by controlling cytoplasmic concentration and extracting mistargeted and orphan species.
A novel bacterial deubiquitinase with multiple chain types specificity regulates the association of ubiquitinated proteins on the phagosome of Legionella pneumophila.
