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Hsp90: from structure to phenotype

Nature Structural & Molecular Biology volume 11, pages 1152–1155 (2004)Cite this article

A recent international conference focused on Hsp90, a molecular chaperone that plays a critical role in a diverse array of cellular processes including the assembly and maturation of some important 'client' proteins, many of which are involved in signal transduction.

Hsp90 is a large, homodimeric protein with three main structural domains4. The N-terminal domain contains the ATP- and geldanamycin-binding site, and is responsible for the weak intrinsic ATPase activity of Hsp90. The middle domain, which is thought to be the major site of client protein binding, is connected to the N-terminal domain through a highly charged linker region. The C-terminal domain contains the dimerization interface and a conserved C-terminal MEEVD motif, which is responsible for binding TPR-containing cochaperones. Cytosolic Hsp90 binds to many other proteins (collectively termed cochaperones) that regulate its activity and form part of the Hsp90 assembly machine (Fig. 1). In contrast to many other molecular chaperones, Hsp90 acts on a specific set of client proteins.

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Figure 1: Cytosolic Hsp90 and its homologs Grp94, TRAP and HTPG along with numerous cochaperones form the cellular assembly machine.

Notes

  1. *The EMBO workshop and second international conference on the Hsp90 Chaperone Machine was held in Gwatt, Switzerland, 25–29 September, 2004. For other information about the conference, see http://www.hsp90.org.

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Authors and Affiliations

  1. Chemistry Department, Cambridge University, Lensfield Road, Cambridge, CB2 1EW, UK

    Sophie E Jackson

  2. Bauer Center for Genomics Research, Harvard University, Cambridge, 02138, Massachusetts, USA

    Christine Queitsch

  3. Department of Biochemistry and Molecular Biology, Mayo Clinic, College of Medicine, 200 First Street SW, Rochester, 55905, Minnesota, USA

    David Toft

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Jackson, S., Queitsch, C. & Toft, D. Hsp90: from structure to phenotype. Nat Struct Mol Biol 11, 1152–1155 (2004). https://doi.org/10.1038/nsmb1204-1152

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