Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …

The eukaryotic cell is a bustling collection of macromolecules acting cooperatively to
mediate the functions required for cell viability. Specific, context-dependent and tightly …

The N-degron pathway targets proteins that bear a destabilizing residue at the N terminus
for proteasome-dependent degradation. In yeast, Ubr1—a single-subunit E3 ligase—is …

Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases
regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry …

The N‐end rule relates the regulation of the in vivo half‐life of a protein to the identity of its N‐
terminal residue. Degradation signals (degrons) that are targeted by the N‐end rule pathway …

AAA+ family proteolytic machines (ClpXP, ClpAP, ClpCP, HslUV, Lon, FtsH, PAN/20S, and
the 26S proteasome) perform protein quality control and are used in regulatory circuits in all …

UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for proteasomal
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …

Specificity of eukaryotic protein degradation is determined by E3 ubiquitin ligases and their
selective binding to protein motifs, termed" degrons," in substrates for ubiquitin-mediated …

Macroautophagy mediates the selective degradation of proteins and non-proteinaceous
cellular constituents. Here, we show that the N-end rule pathway modulates …

The N-end rule pathway is a proteolytic system in which N-terminal residues of short-lived
proteins are recognized by recognition components (N-recognins) as essential components …