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The R-SNARE Endobrevin/VAMP-8 Mediates Homotypic Fusion of Early Endosomes and Late Endosomes
Open accessAbstract
Endobrevin/VAMP-8 is an R-SNARE localized to endosomes, but it is unknown in which intracellular fusion step it operates. Using subcellular fractionation and quantitative immunogold electron microscopy, we found that endobrevin/VAMP-8 is present on all membranes known to communicate with early endosomes, including the plasma membrane, clathrin-coated pits, late endosomes, and membranes of thetrans-Golgi network. Affinity-purified antibodies that block the ability of endobrevin/VAMP-8 to form SNARE core complexes potently inhibit homotypic fusion of both early and late endosomes in vitro. Fab fragments were as active as intact immunoglobulin Gs. Recombinant endobrevin/VAMP-8 inhibited both fusion reactions with similar potency. We conclude that endobrevin/VAMP-8 operates as an R-SNARE in the homotypic fusion of early and late endosomes.
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“This complex brings endosomes/phagosomes in close proximity as a prerequisite for fusion (probably involving VAMP7 and 8) (35, 36).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [36]
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Cites
Greene, L., & Tischler, A. S. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.7.2424 · Cited by 5,594
Wessel, D., & Flügge, U. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90782-6 · Cited by 3,997
SNAP receptors implicated in vesicle targeting and fusion
Söllner, T. H., Whiteheart, S. W., Brunner, M., Erdjument‐Bromage, H., Geromanos, S. J., Tempst, P., & Rothman, J. E. (1993) · Nature · doi:10.1038/362318a0 · Cited by 3,239
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417 · cited 1×
“In the neuronal SNARE complex, three Q-SNARE motifs (one contributed by syntaxin and two by SNAP-25) and one R-SNARE motif (contributed by synaptobrevin/VAMP) form an extended helical bundle (Sutton et al., 1998).”
Self-citationMechanisms of intracellular protein transport
Rothman, J. E. (1994) · Nature · doi:10.1038/372055a0 · Cited by 2,267
Wiedenmann, B. J., & Franke, W. W. (1985) · Cell · doi:10.1016/s0092-8674(85)80082-9 · Cited by 1,432
A new method of preparing gold probes for multiple-labeling cytochemistry.
Slot, J. W., & Geuze, H. J. (1985) · PubMed · Cited by 1,403
Membrane fusion and exocytosis.
Jahn, R., & Südhof, T. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.863 · Cited by 1,253
Self-citationEEA1 links PI(3)K function to Rab5 regulation of endosome fusion
Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J.-M., Brech, A., Callaghan, J., Toh, B.-H., Murphy, C., Zerial, M., & Stenmark, H. (1998) · Nature · doi:10.1038/28879 · Cited by 1,133
rab5 controls early endosome fusion in vitro
Gorvel, J., Chavrier, P., Zerial, M., & Gruenberg, J. E. (1991) · Cell · doi:10.1016/0092-8674(91)90316-q · Cited by 1,094
Flagged first, then by citations
Research works printed but not linked: 2
- Fischer von Mollard G., 1994, Eur. J. Cell Biol., 65, 319
- Slot J.W., 1985, Eur. J. Cell Biol., 38, 87
Cited by
Sorted by citations
Items 101–154 of 154
Shiga toxin stimulates clathrin-independent endocytosis of VAMP2/3/8 SNARE proteins
Renard, H., Garcia-Castillo, M. D., Chambon, V., Lamaze, C., & Johannes, L. (2015) · Journal of Cell Science · doi:10.1242/jcs.171116 · Cited by 19
Regulated exocytosis in chromaffin cells and cytotoxic T lymphocytes: How similar are they?
Becherer, U., Medart, M. R., Schirra, C., Krause, E., Stevens, D. R., & Rettig, J. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.04.002 · Cited by 19
Clostridial neurotoxin‐insensitive vesicular SNAREs in exocytosis and endocytosis
Martı́nez-Arca, S., Alberts, P., & Galli, T. (2000) · Biology of the Cell · doi:10.1016/s0248-4900(00)01096-0 · Cited by 19
Chorein Sensitive Dopamine Release from Pheochromocytoma (PC12) Cells
Honisch, S., Fehrenbacher, B., Lebedeva, A., Alesutan, I., Castor, T., Alkahtani, S. H., Alarifi, S. A., Schaller, M., Stournaras, C., & Lang, F. J. W. (2015) · Neurosignals · doi:10.1159/000442599 · Cited by 18
Caspases regulate VAMP-8 expression and phagocytosis in dendritic cells
Ho, Y. H. S., Cai, D. T., Huang, D., Wang, C. C., & Wong, S. H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.028 · Cited by 18
The role of crinophagy in quality control of the regulated secretory pathway
Szenci, G., Csizmadia, T., & Juhász, G. (2023) · Journal of Cell Science · doi:10.1242/jcs.260741 · Cited by 18
Cueto, J. A., Vanrell, M. C., Salassa, B. N., Nola, S., Galli, T., Colombo, M. I., & Romano, P. S. (2016) · Cellular Microbiology · doi:10.1111/cmi.12713 · Cited by 16
Sdmg1 is a component of secretory granules in mouse secretory exocrine tissues
Best, D., & Adams, I. R. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21827 · Cited by 16
Bastow, E. R., Last, K., Golub, S., Stow, J. L., Stanley, A. C., & Fosang, A. (2012) · Biology Open · doi:10.1242/bio.2012547 · Cited by 16
New MAPS for misfolded proteins
Volkmar, N., Fenech, E. J., & Christianson, J. C. (2016) · Nature Cell Biology · doi:10.1038/ncb3381 · Cited by 14
Gómez-Jaramillo, L., Romero-García, R., Jiménez‐Gómez, G., Riegle, L., Ramos-Amaya, A., Brieva, J. A., Kelly-Worden, M. L., & Campos‐Caro, A. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.46 · Cited by 13
Evidence that late-endosomal SNARE multimerization complex is promoted by transmembrane segments
Mascia, L., & Langosch, D. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.12.008 · Cited by 13
A minimal self-organisation model of the Golgi apparatus
Vagne, Q., Vrel, J.-P., & Sens, P. (2020) · eLife · doi:10.7554/elife.47318 · Cited by 12
VAMP8 suppresses the metastasis via DDX5/β-catenin signal pathway in osteosarcoma
Yang, S., Zhou, P., Zhang, L., Xie, X., Zhang, Y., Bo, K., Xue, J., Zhang, W., Liao, F., Xu, P., et al. (2023) · Cancer Biology & Therapy · doi:10.1080/15384047.2023.2230641 · Cited by 11
Characterization of VAMP‐2 in the lung: implication in lung surfactant secretion
Wang, P., Howard, M. D., Zhang, H., Chintagari, N. R., Bell, A., Jin, N., Mishra, A., & Liu, L. (2012) · Cell Biology International · doi:10.1042/cbi20110146 · Cited by 10
Lysosome fusion in cultured mammalian cells
Bright, N. A., Wartosch, L., & Luzio, J. P. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2014.10.029 · Cited by 10
Direct and Indirect Effects of Filamin A on Tau Pathology in Neuronal Cells
Levert, S., Pilliod, J., Aumont, É., Armanville, S., Tremblay, C., Calon, F., & Leclerc, N. M. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03121-w · Cited by 9
SNARE mediates autophagosome–lysosome fusion
Furuta, N., & Amano, A. (2012) · Journal of Oral Biosciences · doi:10.1016/j.job.2012.03.001 · Cited by 9
Hatakeyama, H., Kobayashi, K., & Kanzaki, M. (2022) · iScience · doi:10.1016/j.isci.2022.104164 · Cited by 9
Role of VAMP8/endobrevin in Constitutive Exocytotic Pathway in HeLa Cells
Okayama, M., Arakawa, T., Tanimura, A., Mizoguchi, I., Tajima, Y., & Takuma, T. (2009) · Cell Structure and Function · doi:10.1247/csf.09013 · Cited by 9
VAMP8/Endobrevin is a critical factor for the homotypic granule growth in pancreatic acinar cells
Hammel, I., Wang, C.-C., Hong, W., & Amihai, D. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1400-1 · Cited by 7
VAMP-8 gene variant is associated with increased risk of early myocardial infarction
Gorący, J., Gorący, I., Kaczmarczyk, M., Parczewski, M., Cyryłowski, L., Brykczyński, M., Peregud‐Pogorzelska, M., & Ciechanowicz, A. (2011) · Archives of Medical Science · doi:10.5114/aoms.2011.23409 · Cited by 7
Manipulation of Host Vesicular Trafficking and Membrane Fusion During Chlamydia Infection
Ronzone, E., Wesolowski, J., & Paumet, F. (2012) · InTech eBooks · doi:10.5772/31244 · Cited by 6
Retrograde transport in plants: Circular economy in the endomembrane system
Zouhar, J., Cao, W., Shen, J., & Rojo, E. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151309 · Cited by 5
Unconventional secretion of tau by VAMP8 impacts its intra- and extracellular cleavage
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Pan, H., & Jing, C. (2025) · Inflammation Research · doi:10.1007/s00011-025-02011-w · Cited by 3
The clues offered by SNAREs on the vacuoles of plants and animals
Barozzi, F., Sampaio, M., Pereira, C., & Sansebastiano, G. P. D. (2025) · Frontiers in Plant Science · doi:10.3389/fpls.2025.1599323 · Cited by 2
Indication for differential sorting of the rat v-SNARE splice isoforms VAMP-1a and -1b
Rodepeter, F. R., Wiegand, S., Lüers, H.-G., Bonaterra, G. A., Lowe, A. W., Bette, M., Jacob, R., & Mandić, R. (2017) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0184 · Cited by 2
Multiple overlapping SNARE complexes drive endosome maturation in Drosophila nephrocytes
Hargitai, D., Molnár, M., Rubics, A., Bodor, I., Baukál, D., Nagy, A., Balogh, V., Simon‐Vecsei, Z., Juhász, G., & Lőrincz, P. (2026) · Nature Communications · doi:10.1038/s41467-026-77479-z · Cited by 1
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Liu, Y., Zhang, Y., Zhu, D. Y., Cai, E. P., Choi, D., Schroer, S. A., Lam, P. P. L., Kang, Y., Woo, M., & Gaisano, H. Y. (2012) · Canadian Journal of Diabetes · doi:10.1016/j.jcjd.2012.07.469 · Cited by 1
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Liu, Y., Hong, J., Wang, G., & Mei, Z. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116907 · Cited by 1
Mülverstedt, A. J. (2006) · doi:10.53846/goediss-1797 · Cited by 1
Kunwar, A. J. (2009) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3634 · Cited by 1
Maktura, G. C., Dias, T. L., Zambalde, É. P., Brenha, B. D. F., Amorim, M. R., Santos, L. N., Buscaratti, L. I., Elston, J. G. D. A., Mara, C., Mancini, M. C. S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.13.464225 · Cited by 1
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Kanwar, N. (2007) · doi:10.53846/goediss-3204 · Cited by 1
Membrane trafficking in neurons regulated by new syntaxin 13-interacting proteins
Steiner, P. (2004) · PubMed · doi:10.5075/epfl-thesis-3091
Puzzella, C., & Sebastian, P. (2014)
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Lord, J., Turton, J. C., Braae, A., Barber, I., Medway, C., Brown, K. S., & Morgan, K. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.05.703
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Achuthan, A. A. (2007) · Minerva Access (University of Melbourne)
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Kim, C. Y. (2018) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)
Xu, P., Hankins, H. M., MacDonald, C., Erlinger, S. J., Frazier, M. N., Diab, N. S., Piper, R. C., Jackson, L. P., MacGurn, J. A., & Graham, T. R. (2017) · eLife · doi:10.7554/elife.28342.021
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West, Z. E. (2021) · Queensland University of Technology · doi:10.5204/thesis.eprints.213196
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Zwilling, D. (2005) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3218
Lord, J., & Morgan, K. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7309-1_4
Brandhorst, D., & Jahn, R. (2008) · Springer eBooks · doi:10.1007/978-0-387-39951-5_5
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Schmücker, S., Schöning, S., Wiegand, C., Höfling, S. M., Bollmann, C., Koliwer, J., & von Mollard, G. F. (2026) · PLoS ONE · doi:10.1371/journal.pone.0343070
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Liu, A., Li, Y., Huang, Z., Chen, W., Xu, P., Wei, X., Hu, G., Liu, S., Liu, X., He, Y., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2602991123
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Metadata
- Authors
- Antonin, W., Holroyd, C., Tikkanen, R., Höning, S., & Jahn, R.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- University of Bonn (DE)
- University of Göttingen (DE)
- Venue
- Molecular Biology of the Cell
- Published
- 2000-10
- Volume
- 11
- Issue
- 10
- Pages
- 3289-3298
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC14992
- OpenAlex
- W2148157392
- Cited by
- 156
- References
- 60
- Citations by year
- 2026: 3 · 2025: 3 · 2023: 3 · 2022: 3 · 2021: 5 · 2020: 4 · 2019: 1 · 2018: 6 · 2017: 10 · 2016: 5 · 2015: 8 · 2014: 6 · 2013: 5 · 2012: 14
- FWCI
- 1.92
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- National Science Foundation
- Deutsche Forschungsgemeinschaft
- 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
- R-SNARE, homotypic fusion, early endosomes, late endosomes, membrane trafficking, clathrin-coated pits, trans-Golgi network, endosomal membrane fusion
- MeSH terms
- Animals, Cell Fractionation, Cell Membrane, Cell-Free System, Coated Pits, Cell-Membrane, Membrane Fusion, Membrane Proteins, Endosomes, Synaptophysin, trans-Golgi Network, Vesicular Transport Proteins, SNARE Proteins, R-SNARE Proteins, Qa-SNARE Proteins, Rats
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