Perception of stress and the mechanisms of molecular chaperones
Our research is focused on molecular chaperones, proteins that assist the (un)folding of other proteins in the cell. Many molecular chaperones are stress-induced proteins. During and following stress, such as heat-shock, they are involved in the prevention of protein misfolding and aggregation in the cell. Hence, the chaperone network provides central mechanisms for the protection and the recovery from damaged proteins in prokaryotes and eukaryotes.
We are also interested in the mechanism for perception of heat-stress in plants. Plants need to rapidly detect mild temperature increments and develop thermotolerance by establishing appropriate molecular defenses against upcoming noxious temperatures. We found strong biochemical evidence that specific plasma membrane calcium channels act as the most upstream heat-sensors in the moss Physcomitrella patens. Currently, we are studying plant genes that are involved in the initial sensing of higher temperatures.
Our long-term goal is to understand heat-shock signaling and chaperone network, in order to prevent protein misfolding and promote the active curing of toxic protein aggregates, especially in the case of protein misfolding diseases.
- Emerging fields in chaperone proteins: A French workshop
Mileo, Elisabetta; Ilbert, Marianne; Barducci, Alessandro; et al.
BIOCHIMIE 151:159-165 10.1016/j.biochi.2018.06.004 AUG 2018
- Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins
Goloubinoff, Pierre; Sassi, Alberto S.; Fauvet, Bruno; et al.
NATURE CHEMICAL BIOLOGY 14(4): 388-+ 10.1038/s41589-018-0013-8 APR 2018
- The growing world of small heat shock proteins: from structure to functions
Carra, Serena; Alberti, Simon; Arrigo, Patrick A.; et al.
CELL STRESS & CHAPERONES, 22 (4): 601-611 10.1007/s12192-017-0787-8 JUL 2017
- Cadmium causes misfolding and aggregation of cytosolic proteins in yeast.
Jacobson T., Priya S., Sharma SK., Andersson S., Jakobsson S., Tanghe R., Ashouri A., Rauch S., Goloubinoff P., Christen P. and Tamás MJ.
Mol Cell Biol. 2017 Aug 11;37(17). pii: e00490-16. DOI:10.1128/MCB.00490-16
- Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling
De Los Rios, Paolo; Goloubinoff, Pierre
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 23 (9): 766-769 10.1038/nsmb.3283 SEP 2016 (Details)
- Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span
Gat-Yablonski, Galia; Finka, Andrija; Pinto, Galit; et al.
AGING-US, 8 (8): 1735-1758 10.18632/aging.101009 AUG 2016
- Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes
Finka, Andrija; Mattoo, Rayees U. H.; Goloubinoff, Pierre
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 85: 715-742 2016 Review; Book Chapter (Details)
- Plant temperature sensing and acquired thermotolerance
- Chaperone unfolding mechanism
- Disaggregation of toxic alpha synuclein oligomers by chaperones