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Originally published as MBC in Press, 10.1091/mbc.E05-12-1096 on May 10, 2006

Vol. 17, Issue 8, 3494-3507, August 2006

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The Hsp90 Chaperone Complex Regulates GDI-dependent Rab Recycling

Christine Y. Chen*, and William E. Balch*,{dagger},{ddagger}

Departments of *Cell Biology and {dagger}Molecular Biology and {ddagger}The Institute for Childhood and Neglected Disease, The Scripps Research Institute, La Jolla, CA 92037

Submitted December 2, 2005; Revised March 27, 2006; Accepted April 27, 2006
Monitoring Editor: Vivek Malhotra

Rab GTPase regulated hubs provide a framework for an integrated coding system, the membrome network, that controls the dynamics of the specialized exocytic and endocytic membrane architectures found in eukaryotic cells. Herein, we report that Rab recycling in the early exocytic pathways involves the heat-shock protein (Hsp)90 chaperone system. We find that Hsp90 forms a complex with guanine nucleotide dissociation inhibitor (GDI) to direct recycling of the client substrate Rab1 required for endoplasmic reticulum (ER)-to-Golgi transport. ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol. Hsp90 activity is required to form a functional GDI complex to retrieve Rab1 from the membrane. Moreover, we find that Hsp90 is essential for Rab1-dependent Golgi assembly. The observation that the highly divergent Rab GTPases Rab1 involved in ER-to-Golgi transport and Rab3A involved in synaptic vesicle fusion require Hsp90 for retrieval from membranes lead us to now propose that the Hsp90 chaperone system may function as a general regulator for Rab GTPase recycling in exocytic and endocytic trafficking pathways involved in cell signaling and proliferation.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05-12-1096) on May 10, 2006.

Address correspondence to: William E. Balch ( webalch{at}scripps.edu)




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