Cited by 520Cellular transport and secretionAutophagy in Disease and TherapyCalcium signaling and nucleotide metabolism

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Oligomeric Complexes Link Rab5 Effectors with NSF and Drive Membrane Fusion via Interactions between EEA1 and Syntaxin 13

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McBride, Heidi M, Rybin, Vladimir, Murphy, Carol, Giner, Angelika, Teasdale, Rohan, Zerial, Marino·1999·Cell

DOI 10.1016/s0092-8674(00)81966-2

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Abstract

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.

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Authors: McBride, H. M., Rybin, V., Murphy, C., Giner, A., Teasdale, R., & Zerial, M.
Affiliations: European Molecular Biology Laboratory (DE)
University of Ioannina (GR)
Corresponding author: Zerial, Marino
ORCID: McBride, Heidi M
Murphy, Carol
Teasdale, Rohan
Zerial, Marino
Venue: Cell
Publisher: Elsevier BV
Published: 1999-08
Volume: 98
Issue: 3
Pages: 377-386
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)81966-2
OpenAlex: W2126162952
Cited by: 520
References: 65
Citations by year: 2026: 1 · 2025: 3 · 2024: 8 · 2023: 6 · 2022: 3 · 2021: 17 · 2020: 17 · 2019: 10 · 2018: 7 · 2017: 11 · 2016: 12 · 2015: 8 · 2014: 14 · 2013: 21 · 2012: 23
FWCI: 18.39
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5099 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: EEA1, Rabaptin-5, NSF, t-SNARE, membrane fusion, endosome fusion, oligomeric complexes, snares, Rab GTPases, vesicle trafficking, ATPase activity
MeSH terms: Adenosine Triphosphatases, Amino Acid Sequence, Autoantigens, Carrier Proteins, HeLa Cells, Humans, Intracellular Membranes, Membrane Fusion, Membrane Proteins, Models, Biological, Molecular Sequence Data, Oligopeptides, Peptide Fragments, Endosomes, Biosensing Techniques, Zinc Fingers, GTP-Binding Proteins, GTP Phosphohydrolases, rab5 GTP-Binding Proteins, Vesicular Transport Proteins, SNARE Proteins, Qa-SNARE Proteins, N-Ethylmaleimide-Sensitive Proteins

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Oligomeric Complexes Link Rab5 Effectors with NSF and Drive Membrane Fusion via Interactions between EEA1 and Syntaxin 13

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