The study of glycosylphosphatidylinositol-anchored-protein sorting has led to some
surprising new findings and concepts. Evidence is accumulating that, during their delivery to …

Like most other eukaryotes, Saccharomyces cerevisiae harbors a GPI anchoring machinery
and uses it to attach proteins to membranes. While a few GPI proteins reside permanently at …

How the ER-associated degradation (ERAD) machinery accurately identifies terminally
misfolded proteins is poorly understood. For luminal ERAD substrates, this recognition …

Abstract Hypoxia-inducible factor 1 (HIF-1) functions as a master regulator of oxygen
homeostasis in metazoan species. HIF-1 mediates changes in gene transcription in …

A quality-control system surveys the lumen of the endoplasmic reticulum for terminally
misfolded proteins. Polypeptides singled out by this system are ultimately degraded by the …

As more details emerge on the mechanisms that mediate and control intracellular transport,
the molecular basis for variety of human diseases has been revealed. In turn, disease …

ER-associated degradation (ERAD) of glycoproteins depends on dual recognition of protein
misfolding and remodeling of the substrate's N-linked glycans. After recognition, substrates …

The Htm1/EDEM protein has been proposed to act as a" degradation lectin" for endoplasmic
reticulum-associated degradation (ERAD) of misfolded glycoproteins. In this study, we …

Cells must constantly monitor the integrity of their macromolecular constituents. Proteins are
the most versatile class of macromolecules but are sensitive to structural alterations …

Endoplasmic reticulum (ER) quality control mechanisms monitor the folding of nascent
secretory and membrane polypeptides. Immature molecules are actively retained in the …