Publications by Pierre Goloubinoff

Autorepression of yeast Hsp70 cochaperones by intramolecular interactions involving their J-domains

Paolo De Los Rios, Bruno Claude Daniel Fauvet, Adélaïde Alice Mohr, Satyam Tiwari, Mathieu Rebeaud, Pierre Goloubinoff

The 70 kDa heat shock protein (Hsp70) chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) coevolved with Hsp70s to trigger ATP hydrolysis and catalytically upload various substrate polypeptides in ne ...

Elsevier Science Inc2024

Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022

Paolo De Los Rios, Wei Li, Pierre Goloubinoff

The Second International Symposium on Cellular and Organismal Stress Responses took place virtually on September 8-9, 2022. This meeting was supported by the Cell Stress Society International (CSSI) and organized by Patricija Van OostenHawle and Andrew Tru ...

SPRINGER2023

A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

Paolo De Los Rios, Bruno Claude Daniel Fauvet, Salvatore Assenza, Satyam Tiwari, Pierre Goloubinoff

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 PORTFOLIO2022

Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control

Paolo De Los Rios, Bruno Claude Daniel Fauvet, Satyam Tiwari, Mathieu Rebeaud, Pierre Goloubinoff

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 SA2021

Function, evolution, and structure of J-domain proteins

Paolo De Los Rios, Alessandro Barducci, Pierre Goloubinoff

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, ...

2019

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

Paolo De Los Rios, Bruno Claude Daniel Fauvet, Alessandro Barducci, Alberto Stefano Sassi, Pierre Goloubinoff

During and after protein translation, molecular chaperones require ATP hydrolysis to favor the native folding of their substrates and, under stress, to avoid aggregation and revert misfolding. Why do some chaperones need ATP, and what are the consequences ...

2018

Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins

Paolo De Los Rios, Bruno Claude Daniel Fauvet, Alessandro Barducci, Alberto Stefano Sassi, Pierre Goloubinoff

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 ...

2017

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

Andrija Finka, Pierre Goloubinoff

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

Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

Paolo De Los Rios, Pierre Goloubinoff

Forceful unfolding by entropic pulling is the general mechanism by which Hsp70 and Hsp110 chaperones control the oligomeric states, structures and activities of cellular proteins. ...

2016

Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs

Paolo De Los Rios, Andrija Finka, Vishal Sood, Pierre Goloubinoff

Classic semiquantitative proteomic methods have shown that all organisms respond to a mild heat shock by an apparent massive accumulation of a small set of proteins, named heat-shock proteins (HSPs) and a concomitant slowing down in the synthesis of the ot ...

Springer2015

Protein folding: Chaperoning protein evolution

Paolo De Los Rios, Pierre Goloubinoff

2012

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate

Paolo De Los Rios, Pierre Goloubinoff

During mild heat-stress, a native thermolabile polypeptide may partially unfold and transiently expose water-avoiding hydrophobic segments that readily tend to associate into a stable misfolded species, rich in intra-molecular non-native beta-sheet structu ...

2011

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

Paolo De Los Rios, Pierre Goloubinoff

Hsp70-Hsp40-NEF and possibly Hsp100 are the only known molecular chaperones that can use the energy of ATP to convert stably pre-aggregated polypeptides into natively refolded proteins. However, the kinetic parameters and ATP costs have remained elusive be ...

Nature Publishing Group2010

Stable -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones

Giovanni Dietler, Mounir Driss Mensi, Hilal Lashuel, Pierre Goloubinoff

alpha-Synuclein aggregation and accumulation in Lewy bodies are implicated in progressive loss of dopaminergic neurons in Parkinson disease and related disorders. In neurons, the Hsp70s and their Hsp40-like J-domain co-chaperones are the only known compone ...

2010

Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants

Jean-Paul Schwitzguebel, Pierre Goloubinoff

The ability to detect early molecular responses to various chemicals is central to the understanding of biological impact of pollutants in a context of varying environmental cues. To monitor stress responses in a model plant, we used transgenic moss Physco ...

2007

The mechanism of Hsp70 chaperones: (entropic) pulling the models together

Paolo De Los Rios, Pierre Goloubinoff

Elsevier2007

Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling

Paolo De Los Rios, Pierre Goloubinoff

National Academy of Sciences2006