Structure and function of molecular chaperones

JMValpuesta

 

José María Valpuesta

Group Leader

Contact

 

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.

 

 

Publications

Sousa R, Liao HS, Cuéllar J, Jin S, Valpuesta JM, Jin AJ, Lafer EM. Clathrin Coat Disassembly Illuminates the Mechanisms of Hsp70 Force Generation. Nat Struct Mol Biol 2016; 23: 821-829

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

Serna M, Carranza G, Martín-Benito J, Janowski R, Canals A, Coll M, Zabala JC, Valpuesta JM. The structure of the complex between α‐tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism. J Cell Sci 2015; 128: 1824–1834

Plimpton RL, Cuéllar J, Lai CW, Aoba T, Makaju A, Franklin S, Mathis AD, Prince JT, Carrascosa JL, Valpuesta JM, Willardson BM. Structures of the Gβ-CCT and PhLP1–Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly. Proc Natl Acad Sci USA 2015; 112: 2413-2418

Chen SW, Drakulic S, Deas E, Ouberai M, Aprile FA, Arranz R, Ness S, Roodveldt C, Guilliams T, De-Genst EJ, Klenerman D, Wood NW, Knowles TP, Alfonso C, Rivas G, Abramov AY, Valpuesta JM, Dobson CM, Cremades N. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation. Proc Natl Acad Sci USA 2015; 112: E1994-2003

 

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 co-chaperones.

 

Figura2

 

grupoValpuestaRed

 

Name
Position
Contact
José María Valpuesta Principal investigator
Jorge Cuéllar Senior scientist
Rosario Fernández Senior scientist
Lucía Quintana Predoctoral scientist
Teresa Bueno Predoctoral scientist
Marcos Gragera Predoctoral scientist
Lissette Ochoa Predoctoral scientist
Moisés Maestro Predoctoral scientist
Virginia Rodríguez Technician

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