Publication
Specificity and Regulation of the Endoplasmic Reticulum-Associated Degradation Machinery
Publications associées (42)
Regulation of Endoplasmic Reticulum Architecture by Protein S-Palmitoylation
The endoplasmic reticulum (ER) is the largest organelle in mammalian cells. More than 50 years ago, its morphology was already described as consisting of two major compartments: the rough ER and the smooth ER, which both fulfil precise and distinct functio ...
EPFL2017Experimental 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 Reviews2016Ubiquitin-dependent folding of the Wnt signaling coreceptor LRP6
Françoise Gisou van der Goot Grunberg, Laurence Gouzi Abrami, Béatrice Kunz, Michal Feldman Elmalam, Elsa Anne Perrody
Many membrane proteins fold inefficiently and require the help of enzymes and chaperones. Here we reveal a novel folding assistance system that operates on membrane proteins from the cytosolic side of the endoplasmic reticulum (ER). We show that folding of ...
Elife Sciences Publications Ltd2016Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone
Françoise Gisou van der Goot Grunberg
Ubiquitin-specific protease 19 (USP19) is one of the deubiquitinating enzymes (DUBs) involved in regulating the ubiquitination status of substrate proteins. There are two major isoforms of USP19 with distinct C-termini; the USP19_a isoform has a transmembr ...
Public Library of Science2016Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides
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 Biology2015A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue
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 Biology2015N-linked sugar-regulated protein folding and quality control in the ER
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 Ltd2015Proteostasis: Bad news and good news from the endoplasmic reticulum
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 Ltd2014Autoadaptive ER-Associated Degradation Defines a Preemptive Unfolded Protein Response Pathway
Maurizio Molinari, Riccardo Bernasconi
Folding-defective proteins must be cleared efficiently from the endoplasmic reticulum (ER) to prevent perturbation of the folding environment and to maintain cellular proteostasis. Misfolded proteins engage dislocation machineries (dislocons) built around ...
Cell Press2013A Biochemical and Biophysical Investigation of 5-HT3 Receptor Stability
The 5-hydroxytryptamine 3 receptor (5-HT3R) is a member of the pentameric ligand-gated ion channel (pLGIC) family, that plays an important role in fast signal transduction and cell-cell communication in synapses: They convert a chemical signal from a neuro ...
EPFL2012