Maintenance of ubiquitin homeostasis is essential for proper control of the size of postsynaptic density and the growth of specialized membrane structure.
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.
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.
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.
A novel regulatory step in the endocytic pathway, which occurs post-internalization, takes place at the trans-Golgi network and involves the arrestin-related protein Rod1 and the ubiquitin ligase Rsp5.
