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

Cell | Aug 6, 1999

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 RIS Download

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