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First published online 12 February 2008
doi: 10.1242/jcs.015610

Journal of Cell Science 121, 717-723 (2008)
Published by The Company of Biologists 2008
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Research Article

A novel HSP90 chaperone complex regulates intracellular vesicle transport

Gregor P. Lotz1,*, Alexander Brychzy2, Stefan Heinz3 and Wolfgang M. J. Obermann1,4,{ddagger}

1 Protein Folding Group, Institute for Genetics, University of Bonn, Römerstr. 164, 53117 Bonn, Germany
2 Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
3 Institute for Transfusion Medicine and Immunohematology, Red Cross Blood Donor Service Baden-Württemberg/Hessen, Sandhofstr. 1, 60528 Frankfurt, Germany
4 Department of Neuroscience and Cell Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston TX 77555, USA

{ddagger} Author for correspondence (e-mail: wmoberma{at}utmb.edu)

Accepted 11 December 2007

Heat shock protein 90 (HSP90) is considered a specialized molecular chaperone that controls the folding of cell-regulatory proteins such as steroid receptors and kinases. However, its high abundance is suggestive of a more general function in other fundamental processes. Here, we show that HSP90 is required for vesicular protein transport in the cell. We have identified a novel chaperone complex comprising HSP90 and TPR1 that is recruited to the membrane protein VAP-33. Depletion of the TPR1 protein in mammalian cells inhibits transport of vesicular stomatitis virus glycoprotein (VSVG) and leads to accumulation of this cargo protein in the Golgi apparatus. Furthermore, trafficking of VSVG between Golgi stacks is dependent on the ATPase function of HSP90 and can be inhibited by drugs specific for HSP90. Our results identify a new role for HSP90 in protein sorting, pointing to a central role for this molecular chaperone in the cell.

Key words: HSP90, Molecular chaperones, Protein folding, Radicicol






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