A Novel Tetanus Neurotoxin-insensitive Vesicle-associated Membrane Protein in SNARE Complexes of the Apical Plasma Membrane of Epithelial Cells

Autor: Heiner Niemann, Graça Raposo, Jian Min Tian, Michael Karin, Ahmed Zahraoui, V. V. Vaidyanathan, Thierry Galli, Daniel Louvard
Rok vydání: 1998
Předmět:
Botulinum Toxins
DNA
Complementary
Synaptosomal-Associated Protein 25
Vesicle-Associated Membrane Protein 3
Molecular Sequence Data
Vesicular Transport Proteins
Syntaxin 1
Nerve Tissue Proteins
Biology
Article
R-SNARE Proteins
Cell membrane
Tetanus Toxin
medicine
Animals
Humans
Amino Acid Sequence
Qc-SNARE Proteins
Enzyme Inhibitors
Molecular Biology
VAMP3
Base Sequence
Sequence Homology
Amino Acid
Qa-SNARE Proteins
Cell Membrane
Membrane Proteins
Metalloendopeptidases
Epithelial Cells
Munc-18
Cell Biology
Qb-SNARE Proteins
Rats
Cell biology
Synaptic vesicle exocytosis
Dithiothreitol
Vesicle-associated membrane protein
medicine.anatomical_structure
nervous system
Ethylmaleimide
Antigens
Surface
Rabbits
Caco-2 Cells
biological phenomena
cell phenomena
and immunity
Carrier Proteins
SNARE Proteins
Zdroj: Molecular Biology of the Cell. 9:1437-1448
ISSN: 1939-4586
1059-1524
DOI: 10.1091/mbc.9.6.1437
Popis: The importance of soluble N-ethyl maleimide (NEM)-sensitive fusion protein (NSF) attachment protein (SNAP) receptors (SNAREs) in synaptic vesicle exocytosis is well established because it has been demonstrated that clostridial neurotoxins (NTs) proteolyze the vesicle SNAREs (v-SNAREs) vesicle-associated membrane protein (VAMP)/brevins and their partners, the target SNAREs (t-SNAREs) syntaxin 1 and SNAP25. Yet, several exocytotic events, including apical exocytosis in epithelial cells, are insensitive to numerous clostridial NTs, suggesting the presence of SNARE-independent mechanisms of exocytosis. In this study we found that syntaxin 3, SNAP23, and a newly identified VAMP/brevin, tetanus neurotoxin (TeNT)-insensitive VAMP (TI-VAMP), are insensitive to clostridial NTs. In epithelial cells, TI-VAMP–containing vesicles were concentrated in the apical domain, and the protein was detected at the apical plasma membrane by immunogold labeling on ultrathin cryosections. Syntaxin 3 and SNAP23 were codistributed at the apical plasma membrane where they formed NEM-dependent SNARE complexes with TI-VAMP and cellubrevin. We suggest that TI-VAMP, SNAP23, and syntaxin 3 can participate in exocytotic processes at the apical plasma membrane of epithelial cells and, more generally, domain-specific exocytosis in clostridial NT-resistant pathways.
Databáze: OpenAIRE
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