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A new functional domain of guanine nucleotide dissociation inhibitor (alpha-gdi) involved in rab recycling

Academic Article
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Overview

authors

  • Luan, P.
  • Heine, A.
  • Zeng, K.
  • Moyer, B.
  • Greasely, S. E.
  • Kuhn, Peter
  • Balch, William E.
  • Wilson, Ian

publication date

  • March 2000

journal

  • Traffic  Journal

abstract

  • Guanine nucleotide dissociation inhibitor (GDI) is a 55-kDa protein that functions in vesicular membrane transport to recycle Rab GTPases. We have now determined the crystal structure of bovine alpha-GDI at ultra-high resolution (1.04 A). Refinement at this resolution highlighted a region with high mobility of its main-chain residues. This corresponded to a surface loop in the primarily alpha-helical domain II at the base of alpha-GDI containing the previously uncharacterized sequence-conserved region (SCR) 3A. Site-directed mutagenesis showed that this mobile loop plays a crucial role in binding of GDI to membranes and extraction of membrane-bound Rab. This domain, referred to as the mobile effector loop, in combination with Rab-binding residues found in the multi-sheet domain I at the apex of alpha-GDI may provide flexibility for recycling of diverse Rab GTPases. We propose that conserved residues in domains I and II synergize to form the functional face of GDI, and that domain II mediates a critical step in Rab recycling during vesicle fusion.

subject areas

  • Amino Acid Motifs
  • Animals
  • Cattle
  • Crystallography, X-Ray
  • Cytosol
  • Fungal Proteins
  • Guanine Nucleotide Dissociation Inhibitors
  • Intracellular Membranes
  • Models, Molecular
  • Motion
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein Transport
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Structure-Activity Relationship
  • Transport Vesicles
  • rab1 GTP-Binding Proteins
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Research

keywords

  • GDI
  • Rab
  • fusion
  • transport
  • vesicle
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Identity

International Standard Serial Number (ISSN)

  • 1398-9219

Digital Object Identifier (DOI)

  • 10.1034/j.1600-0854.2000.010309.x

PubMed ID

  • 11208110
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Additional Document Info

start page

  • 270

end page

  • 281

volume

  • 1

issue

  • 3

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