The DOI matches its Crossref record; 64 of the 65 references it cites were found in a registry or an index.
Oligomeric Complexes Link Rab5 Effectors with NSF and Drive Membrane Fusion via Interactions between EEA1 and Syntaxin 13
Open accessAbstract
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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“The small GTPase Rab5A is a marker of early phagosomes and facilitates downstream maturation by recruiting early endosomal antigen 1 (EEA1), which then binds NSF, Rabex5, and Rabaptin-5 and subsequently syntaxin13 to form a fusogenic complex with endosomes (22–24).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [22]
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Cites
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Self-citationThe Rab5 effector EEA1 is a core component of endosome docking
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Study of the role of Rab proteins and their effectors on Tunneling nanotubes
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Mécanismes de tri et voies de transport intracellulaire des protéines de la membrane du lysosome
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Mécanismes moléculaires du transport de la leptine par les tanycytes hypothalamiques
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Role of vSNAREs in post-synaptic AMPAR trafficking, glutamatergic transmisson and plasticity
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Functional characterization of the Rab11A-dependent secretory pathway in Toxoplasma gondii
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Metadata
- 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
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-08
- Volume
- 98
- Issue
- 3
- Pages
- 377-386
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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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