Publication
Three branches to rule them all? UPR signalling in response to chemically versus misfolded proteins-induced ER stress
Publications associées (38)
Why do we need so many proteins? A physical insight into the collaboration of Hsp70 and DnaJ
The Hsp70 cycle is a key element of protein homeostasis, which is essential to avoid protein aggregation and protein-related diseases. Despite many experimental observations of the interaction between Hsp70, its co-chaperone DnaJ and various substrates, li ...
EPFL2023A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70
Paolo De Los Rios, Pierre Goloubinoff, Satyam Tiwari, Bruno Claude Daniel Fauvet, Salvatore Assenza
Detailed understanding of the mechanism by which Hsp70 chaperones protect cells against protein aggregation is hampered by the lack of a comprehensive characterization of the aggregates, which are typically heterogeneous. Here we designed a reporter chaper ...
NATURE PORTFOLIO2022Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the UPR in models of neurodegeneration
Alteration to endoplasmic reticulum (ER) proteostasis is observed in a variety of neurodegenerative diseases associated with abnormal protein aggregation. Activation of the unfolded protein response (UPR) enables an adaptive reaction to recover ER proteost ...
2021Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control
Paolo De Los Rios, Pierre Goloubinoff, Satyam Tiwari, Mathieu Rebeaud, Bruno Claude Daniel Fauvet
Life is a non-equilibrium phenomenon. Owing to their high free energy content, the macromolecules of life tend to spontaneously react with ambient oxygen and water and turn into more stable inorganic molecules. A similar thermodynamic picture applies to th ...
FRONTIERS MEDIA SA2021Overexpression of transcription factor Foxa1 and target genes remediate therapeutic protein production bottlenecks in Chinese hamster ovary cells
Nicolas Mermod, Iris Bodenmann
Despite extensive research conducted to increase protein production from Chinese hamster ovary (CHO) cells, cellular bottlenecks often remain, hindering high yields. In this study, a transcriptomic analysis led to the identification of 32 genes that are co ...
WILEY2020Thioredoxin-Related Transmembrane Proteins: TMX1 and Little Brothers TMX2, TMX3, TMX4 and TMX5
The endoplasmic reticulum (ER) is site of synthesis and maturation of membrane and secretory proteins in eukaryotic cells. The ER contains more than 20 members of the Protein Disulfide Isomerase (PDI) family. These enzymes regulate formation, isomerization ...
2020Non equilibrium thermodynamics of protein organization
Three quarters of the thesis will be devoted to the discussion of non equilibrium systems.
We show how certain biological systems cannot be described by standard thermodynamics.
The reason is that the energy consumption due to the hydrolysis of ATP imposes ...
EPFL2018Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins
Paolo De Los Rios, Alessandro Barducci, Pierre Goloubinoff, Bruno Claude Daniel Fauvet, Alberto Stefano Sassi
Protein homeostasis, namely the ensemble of cellular mechanisms collectively controlling the activity, stability and conformational states of proteins, depends on energy-consuming processes. De novo protein synthesis requires ATP hydrolysis for peptide bon ...
2017Investigating the Biological Mechanisms underlying the Initiation of Autoimmunity against Beta Cell Antigens in Type 1 Diabetes
Type 1 diabetes (T1D) is an autoimmune disease characterized by circulating autoantibodies, lymphocytic infiltration of pancreatic islets of Langerhans, and cell-specific destruction of beta cells, leading to insulin deficiency and symptomatic hyperglycemi ...
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 Reviews2016