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The Hsp90 chaperone complex regulates GDI-dependent Rab recycling

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Overview

authors

  • Chen, C. Y.
  • Balch, William E.

publication date

  • August 2006

journal

  • Molecular Biology of the Cell  Journal

abstract

  • 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.

subject areas

  • Animals
  • Brefeldin A
  • CHO Cells
  • Cattle
  • Cell Membrane
  • Cells, Cultured
  • Cricetinae
  • Cricetulus
  • Endoplasmic Reticulum
  • Gene Expression
  • Golgi Apparatus
  • Guanine Nucleotide Dissociation Inhibitors
  • HSP90 Heat-Shock Proteins
  • Humans
  • Models, Biological
  • Multiprotein Complexes
  • Protein Binding
  • Protein Transport
  • Rats
  • rab1 GTP-Binding Proteins
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Identity

PubMed Central ID

  • PMC1525227

International Standard Serial Number (ISSN)

  • 1059-1524

Digital Object Identifier (DOI)

  • 10.1091/mbc.E05-12-1096

PubMed ID

  • 16687576
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Additional Document Info

start page

  • 3494

end page

  • 3507

volume

  • 17

issue

  • 8

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