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MBC in Press, published online ahead of print May 10, 2006
Mol. Biol. Cell 10.1091/mbc.E05-12-1096

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Submitted on December 2, 2005
Revised on March 27, 2006
Accepted on April 27, 2006

The Hsp90 Chaperone Complex Regulates GDI-dependent Rab Recycling

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

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

Monitoring Editor: Vivek Malhotra

Rab GTPase regulated hubs provide a framework for an integrated coding system, the membrome network (Gurkan et al. (2005) Mol. Biol. Cell, 16:3847), 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 Hsp90 cochaperone 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 (Sakisaka et al. (2002) EMBO J., 21: 6125) 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.

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




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