Maintaining proteome integrity is essential for long-term viability of all organisms and is
overseen by intrinsic quality control mechanisms. The secretory pathway of eukaryotes …

Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates
governs numerous eukaryotic cellular processes, including apoptosis, cell division and …

Ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes
responsible for the attachment of ubiquitin (Ub) to cellular proteins. Humans have∼ 40 E2s …

Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

Protein folding is inherently error prone, especially in the endoplasmic reticulum (ER). Even
with an elaborate network of molecular chaperones and protein folding facilitators …

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of
ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct …

RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins,
constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin …

The post-translational modification of proteins regulates many biological processes. Their
dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications …

Mistakes are part of our world and constantly occurring. Due to transcriptional and
translational failures, genomic mutations or diverse stress conditions like oxidation or heat …

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 …