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HSP90 and the R2TP co-chaperone complex: building multi-protein machineries essential for cell growth and gene expression

Boulon, S.; Bertrand*, E.; Pradet-Balade*, B.

RNA Biol

2012-02 / vol 9 / pages 148-54

Abstract

HSP90 (Heat Shock Protein 90) is an essential chaperone involved in the last folding steps of client proteins. It has many clients, and these are often recognized through specific adaptors. Recently, the conserved R2TP complex was identified as a key HSP90 co-chaperone. Current evidences indicate that the HSP90/R2TP system assembles multi-molecular protein complexes. Strikingly, these comprise basic machineries of gene expression: (1) nuclear RNA polymerases; (2) the snoRNPs, essential to produce ribosomes; and (3) mTOR Complex 1 and 2, which control translational activity and cell growth. Another important substrate is the telomerase RNP, required for continuous cell proliferation. We discuss here the assembly of RNA polymerases in bacteria and eukaryotes, the role of HSP90/R2TP in this process and in the assembly of snoRNPs and the PIKK family of TORC1 kinase. Finally, we speculate on the roles of R2TP as a master regulator of cell growth under normal or pathological conditions.

Lire sur PubMed

10.4161/rna.18494 18494 [pii]

1555-8584 (Electronic) 1547-6286 (Linking)

IGMM team(s) involved in this publication
Étiquettes

*Gene Expression Regulation; Cell Proliferation; Models, Biological; RNA Polymerase II/metabolism; Molecular Chaperones/metabolism; Protein Binding; Multiprotein Complexes/metabolism; HSP90 Heat-Shock Proteins/*metabolism; Nuclear Proteins/*metabolism; Ribonucleoproteins, Small Nucleolar/metabolism

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