Structure and function of molecular chaperones

2021 JMV


José María Valpuesta

Group Leader



Research summary

Our group has been working over the last years in the structural characterisation of large macromolecular complexes, among them some molecular chaperones, which are proteins that assist the folding of other proteins.




Cuéllar J, Ludlam WG, Tensmeyer, NC, Aoba T, Dhavale M, Bueno T, Santiago C, Plimpton RL, Makaju A, Franklin S, Willardson BM, Valpuesta JM.Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly. Nature Communications 2019; 10:2865 doi:10.1038/s41467-019-10781-1

Campos LA, Sharma R, Alvira S, Ruiz FM, Ibarra-Molero B, Sadqi M, Alfonso C, Rivas G, Sanchez-Ruiz JM, Romero A, Valpuesta JM, Muñoz V. Engineering Protein Assemblies with Allosteric Control via Monomer Fold-Switching. Nature Communications 2019; 10:5703

Esteve P, Rueda-Carrasco J, Inés Mateo M, Martin-Bermejo MJ, Draffin J, Pereyra G, Sandonís A, Crespo I, Moreno I, Aso E, Garcia-Esparcia P, Gomez-Tortosa E, Rabano A, Fortea J, Alcolea D, Lleo A, Heneka MT, Valpuesta JM, Esteban JA, Ferrer I, Dominguez M, Bovolenta P. Elevated levels of Secreted-Frizzled-Related-Protein 1 contribute to Alzheimer’s disease pathogenesis. Nature Neuroscience 2019; doi: 10.1038/s41593-019-0432-1.

Quintana-Gallardo L, Martín-Benito J, Marcilla M, Espadas G, Sabidó E, Valpuesta JM. The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism. Scientific Reports 2019; 9:5102

Ukleja M, Cuellar J, Siwaszek A, Kasprzak JM, Czarnocki-Cieciura M, Bujnicki JM, Dziembowski A, Valpuesta JM. The architecture of the Schizosaccharomyces pombe CCR4-NOT complex. Nat Commun 2016; 7:10433


Most cell processes are executed by sets of proteins that work like molecular machines in a coordinated manner, thus acting as an assembly line and making the process more efficient. One such assembly line is that formed by molecular chaperones, a group of proteins involved in cell homeostasis through two opposite functions, protein folding and degradation. In recent years, it was found that chaperones are not only devoted to assisting the folding of other proteins but also, in certain conditions, that they can be active players in protein degradation. The two processes are carried out through the transient formation of complexes between different chaperones and co-chaperones. Our goal is the structural characterization of some of these complexes, with the aim of understanding the structural mechanisms by which they function. To this end, we are using electron microscopy and image processing techniques as our main tools, and combining the information obtained with these techniques with the available atomic structures of some of these chaperones and cochaperones.






José María Valpuesta Principal investigator
Jorge Cuéllar Senior scientist
Lissette Ochoa Predoctoral scientist
Moisés Maestro Predoctoral scientist
Sergio Pipaón Predoctoral scientist
Carmen Majano Predoctoral scientist
Virginia Rodríguez Technician

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