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UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum

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Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Pierre Goloubinoff, Andrija Finka

Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can bind a ...

Annual Reviews2016

Five Questions (with their Answers) on ER-Associated Degradation

Maurizio Molinari

Production of a functional proteome is a major burden for our cells. Native proteins operate inside and outside the cells to eventually warrant life and adaptation to metabolic and environmental changes, there is no doubt that production and inappropriate ...

Wiley-Blackwell2016

Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery

Maurizio Molinari

The endoplasmic reticulum (ER) is a site of protein biogenesis in eukaryotic cells. Perturbing ER homeostasis activates stress programs collectively called the unfolded protein response (UPR). The UPR enhances production of ER-resident chaperones and enzym ...

Nature Publishing Group2016

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Cellular functions are largely regulated by reversible post-translational modifications of proteins which act as switches. Amongst these, S-palmitoylation is unique in that it confers hydrophobicity. Due to technical difficulties, the understanding of this ...

Public Library of Science2016

Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the lectin chaperone malectin possibly involved in a first triage of defective ...

Academic Press Ltd- Elsevier Science Ltd2015

Differential dependence on N-glycosylation of anthrax toxin receptors CMG2 and TEM8

Françoise Gisou van der Goot Grunberg, Julie Deuquet Ariosa

ANTXR 1 and 2, also known as TEM8 and CMG2, are two type I membrane proteins, which have been extensively studied for their role as anthrax toxin receptors, but with a still elusive physiological function. Here we have analyzed the importance of N-glycosyl ...

Public Library of Science2015

Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides

Maurizio Molinari

The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. The lumen of the mammalian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ensure formation of the correct ...

Amer Soc Cell Biology2015

Only native polypeptides are released from the endoplasmic reticulum (ER) to be transported at the site of activity. Persistently misfolded proteins are retained and eventually selected for ER-associated degradation (ERAD). The paradox of a structure-based ...

Amer Soc Cell Biology2015

Proteostasis: Bad news and good news from the endoplasmic reticulum

Maurizio Molinari

The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells proteome. The capacity to produce correctly folded polypeptides a ...

E M H Swiss Medical Publishers Ltd2014

The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease

Johan Auwerx, Laurent Mouchiroud, Virginija Jovaisaite

The ability to respond to various intracellular and/or extracellular stresses allows the organism to adapt to changing environmental conditions and drives evolution. It is now well accepted that a progressive decline of the efficiency of stress response pa ...

Company of Biologists2014