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

Misfolded proteins compromise cellular homeostasis. This is especially problematic in the
endoplasmic reticulum (ER), which is a high-capacity protein-folding compartment and …

Vitamin K epoxide reductase (VKOR) drives the vitamin K cycle, activating vitamin K-
dependent blood clotting factors. VKOR is also the target of the widely used anticoagulant …

In endoplasmic reticulum-associated protein degradation (ERAD), membrane proteins are
ubiquitinated, extracted from the membrane, and degraded by the proteasome. The cytosolic …

The Golgi apparatus is essential for protein sorting, yet its quality control mechanisms are
poorly understood. Here we show that the Dsc ubiquitin ligase complex uses its rhomboid …

Triterpene cyclases catalyze the first committed step in triterpene biosynthesis, by forming
mono-to pentacyclic backbone structures from oxygenated C30 isoprenoid precursors …

Transmembrane proteins have unique requirements to fold and integrate into the
endoplasmic reticulum (ER) membrane. Most notably, transmembrane proteins must fold in …

In ER-associated degradation (ERAD), misfolded ER proteins are degraded by the
proteasome after undergoing ubiquitylation. Yeast Doa10 (human MARCHF6/TEB4) is a …

The neuron-specific K+/Cl− co-transporter 2, KCC2, which is critical for brain development,
regulates γ-aminobutyric acid-dependent inhibitory neurotransmission. Consistent with its …

Upon internalization, many surface membrane proteins are recycled back to the plasma
membrane. Although these endosomal trafficking pathways control surface protein activity …