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.
Interaction mapping of ubiquitin ligase complexes embedded in the endoplasmic reticulum membrane has identified interactors of RNF26 that influence innate immune signalling.
The cancer-associated human ubiquitin ligase HUWE1 can adopt an auto-inhibited dimeric state, whose occupancy is regulated by competing intra- and intermolecular interactions of the dimerization region and by the tumor suppressor p14ARF.
The E3 ubiquitin ligase complex linear ubiquitin chain assembly complex (LUBAC) forms a branched chain on linear ubiquitin chains depending on the RING-in-between-RING-type E3 ligase heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1L).
Chemical perturbation-dependent deep mutational scanning data collected by a lab-based interdisciplinary graduate class resolves a paradox between the high evolution conservation and the high mutational tolerance of the protein ubiquitin.
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.
A ubiquitin E3 ligase localizes to focal adhesions at the front of migrating human cells where it regulates cytoskeletal dynamics by targeting a focal adhesion protein.
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.
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.
