ArticleThe EMBO journal2000
Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- The SNARE protein SNAP-25 is required for normal exocytosis at auditory hair cell ribbon synapses.iScience · 2022Article
- Molecular mechanism of fusion pore formation driven by the neuronal SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The fusion pore, 60 years after the first cartoon.FEBS letters · 2018Review
- The destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion.PeerJ · 2015Article
- How could SNARE proteins open a fusion pore?Physiology (Bethesda, Md.) · 2014Review
- Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic.PloS one · 2014Article
- Deciphering dead-end docking of large dense core vesicles in bovine chromaffin cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Association of SNAREs and calcium channels with the borders of cytoskeletal cages organizes the secretory machinery in chromaffin cells.Cellular and molecular neurobiology · 2010Article
- Role of the synaptobrevin C terminus in fusion pore formation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Opposing functions of two sub-domains of the SNARE-complex in neurotransmission.The EMBO journal · 2010Article
- Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis.The Journal of cell biology · 2010Article
- The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Phosphorylation of SNAP-25 at Ser187 mediates enhancement of exocytosis by a phorbol ester in INS-1 cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Physical and functional interactions of SNAP-23 with annexin A2.American journal of respiratory cell and molecular biology · 2007Article
- Phosphomimetic mutation of Ser-187 of SNAP-25 increases both syntaxin binding and highly Ca2+-sensitive exocytosis.The Journal of general physiology · 2007Article
- Docking of secretory vesicles is syntaxin dependent.PloS one · 2006Article
- Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles.The EMBO journal · 2006Article
- Structural transitions in the synaptic SNARE complex during Ca2+-triggered exocytosis.The Journal of cell biology · 2006Article
- v-SNAREs control exocytosis of vesicles from priming to fusion.The EMBO journal · 2005Article
- Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.Molecular biology of the cell · 2005Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The highly conserved SNARE proteins, SNAP-25, syntaxin and synaptobrevin, form a tight ternary complex, which is essential for exocytosis. Crystallization of this complex revealed a four-helix bundle with an unusual hydrophilic layer (zero layer) in its center. In order to evaluate the role of this layer in different kinetic components of secretion, we used the Semliki Forest virus (SFV) system to infect adrenal chromaffin cells with SNAP-25 Q174L, a point mutant in the zero layer. Using combined flash photolysis of caged calcium and membrane capacitance measurements, we investigated its effect on the exocytotic burst and sustained phase of exocytosis with high time resolution. Cells expressing SNAP-25 Q174L displayed a selective reduction in the sustained phase, while the two components of the exocytotic burst remained unaffected. Furthermore, the exocytotic response to the second flash was significantly reduced, indicating a decrease in refilling kinetics. We therefore conclude that the zero layer is critical for the formation of SNARE complexes, but that it plays no role in the dynamic equilibrium between the two exocytosis-competent vesicle pools.
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