Heat-Shock Biology and the Mechanisms of Chaperone Actions

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.

• Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1
  Kumar, V; Peter, JJ; Sagar, A; Ray, A; Jha, MP; Rebeaud, ME; Tiwari, S; Goloubinoff, P; Ashish; Mapa, K
  FEBS JOURNAL, 10.1111/febs.15045  2019
• Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA plus disaggregation machine
  Mazal, H; Iljina, M; Barak, Y; Elad, N; Rosenzweig, R; Goloubinoff, P; Riven, I; Haran, G
  NATURE COMMUNICATIONS, 10 10.1038/s41467-019-09476-6 MAR 29 2019
• ZnJ2 Is a Member of a Large Chaperone Family in the Chloroplast of Photosynthetic Organisms that Features a DnaJ-Like Zn-Finger Domain
  Doron, L; Goloubinoff, P; Shapira, M
  FRONTIERS IN MOLECULAR BIOSCIENCES, 5 10.3389/fmolb.2018.00002 FEB 15 2018
• Function, evolution, and structure of J-domain proteins
  Kampinga, HH; Andreasson, C; Barducci, A; Cheetham, ME; Cyr, D; Emanuelsson, C; Genevaux, P; Gestwicki, JE; Goloubinoff, P; Huerta-Cepas, J; Kirstein, J; Liberek, K; Mayer, MP; Nagata, K; Nillegoda, NB; Pulido, P; Ramos, C; De los Rios, P; Rospert, S;
  Rosenzweig, R; Sahi, C; Taipale, M; Tomiczek, B; Ushioda, R; Young, JC; Zimmermann, R; Zylicz, A; Zylicz, M; Craig, EA; Marszalek, J
  CELL STRESS & CHAPERONES, 24 (1):7-15; 10.1007/s12192-018-0948-4 JAN 2019
• 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

• Plant temperature sensing and acquired thermotolerance
• Chaperone unfolding mechanism

• Disaggregation of toxic alpha synuclein oligomers by chaperones