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Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13.

SNAREs and Rab GTPases cooperate in vesicle transport through a mechanism yet poorly understood. We now demonstrate that the Rab5 effectors EEA1 and Rabaptin-5/Rabex-5 exist on the membrane in high molecular weight oligomers, which also contain NSF. Oligomeric assembly is modulated by the ATPase activity of NSF. Syntaxin 13, the t-SNARE required for endosome fusion, is transiently incorporated into the large oligomers via direct interactions with EEA1. This interaction is required to drive fusion, since both dominant-negative EEA1 and synthetic peptides encoding the FYVE Zn2+ finger hinder the interaction and block fusion. We propose a novel mechanism whereby oligomeric EEA1 and NSF mediate the local activation of syntaxin 13 upon membrane tethering and, by analogy with viral fusion proteins, coordinate the assembly of a fusion pore.

Pubmed ID: 10458612


  • McBride HM
  • Rybin V
  • Murphy C
  • Giner A
  • Teasdale R
  • Zerial M



Publication Data

August 6, 1999

Associated Grants


Mesh Terms

  • Adenosine Triphosphatases
  • Amino Acid Sequence
  • Autoantigens
  • Biosensing Techniques
  • Carrier Proteins
  • Endosomes
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • HeLa Cells
  • Humans
  • Intracellular Membranes
  • Membrane Fusion
  • Membrane Proteins
  • Models, Biological
  • Molecular Sequence Data
  • N-Ethylmaleimide-Sensitive Proteins
  • Oligopeptides
  • Peptide Fragments
  • Qa-SNARE Proteins
  • SNARE Proteins
  • Vesicular Transport Proteins
  • Zinc Fingers
  • rab5 GTP-Binding Proteins