In acute promyelocytic leukaemia (APL), the promyelocytic leukaemia (PML) protein is fused
to the retinoic acid receptor α (RAR). This disease can be treated effectively with arsenic, …

Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3
ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 …

Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function
of proteins involved in diverse cellular processes. SUMO-specific enzymes conjugate …

Mammalian RNF4 is a dimeric RING ubiquitin E3 ligase that ubiquitylates poly-SUMOylated
proteins. We found that RNF4 bound ubiquitin-charged UbcH5a tightly but free UbcH5a …

The Rho-like GTPase, Rac1, induces cytoskeletal rearrangements required for cell migration.
Rac activation is regulated through a number of mechanisms, including control of …

The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite
motif module, composed of a RING domain, one or two B-box domains and a coiled-coil …

The covalent attachment of the protein ubiquitin to intracellular proteins by a process known
as ubiquitylation regulates almost all major cellular systems, predominantly by regulating …

The modification of proteins by SUMO (small ubiquitin-related modifier) plays important
roles in regulating the activity, stability and cellular localization of target proteins. Similar to …

RING E3 ligase–catalyzed formation of K63-linked ubiquitin chains by the Ube2V2–Ubc13
E2 complex is required in many important biological processes. Here we report the structure …

During Caenorhabditis elegans oocyte meiosis, a multi-protein ring complex (RC) localized
between homologous chromosomes, promotes chromosome congression through the action …