ArticleProceedings of the National Academy of Sciences of the United States of America1999
A single amino acid near the C terminus of the synaptosomeassociated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 89 citations in OpenAlex.
- The SNARE protein SNAP-25 is required for normal exocytosis at auditory hair cell ribbon synapses.iScience · 2022Article
- Quantifying neurotransmitter secretion at single-vesicle resolution using high-density complementary metal-oxide-semiconductor electrode array.Nature communications · 2021Article
- Sexual Dimorphism in Stress-induced Hyperthermia in SNAP25Δ3 mice, a mouse model with disabled Gβγ regulation of the exocytotic fusion apparatus.The European journal of neuroscience · 2020Article
- Multiple sclerosis drug FTY-720 toxicity is mediated by the heterotypic fusion of organelles in neuroendocrine cells.Scientific reports · 2019Article
- Disabling the Gβγ-SNARE interaction disrupts GPCR-mediated presynaptic inhibition, leading to physiological and behavioral phenotypes.Science signaling · 2019Article
- 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
- Single-Cell Recording of Vesicle Release From Human Neuroblastoma Cells Using 1024-ch Monolithic CMOS Bioelectronics.IEEE transactions on biomedical circuits and systems · 2018Article
- The fusion pore, 60 years after the first cartoon.FEBS letters · 2018Review
- Therapeutic use of botulinum toxin in pain treatment.Neuronal signaling · 2018Review
- The unfolding landscape of the congenital myasthenic syndromes.Annals of the New York Academy of Sciences · 2018Review
- Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology.Pharmacological reviews · 2017Review
- Gβγ Binds to the Extreme C Terminus of SNAP25 to Mediate the Action of Gi/o-Coupled G Protein-Coupled Receptors.Molecular pharmacology · 2016Article
- Function Suggests Nano-Structure: Quantitative Structural Support for SNARE-Mediated Pore Formation.Neurotoxicity research · 2016Article
- Mutant SNAP25B causes myasthenia, cortical hyperexcitability, ataxia, and intellectual disability.Neurology · 2014Article
- How could SNARE proteins open a fusion pore?Physiology (Bethesda, Md.) · 2014Review
- The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.Cellular and molecular life sciences : CMLS · 2014Review
- Parallel recording of neurotransmitters release from chromaffin cells using a 10×10 CMOS IC potentiostat array with on-chip working electrodes.Biosensors & bioelectronics · 2013Article
- Article
- 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
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amperometry in chromaffin cells expressing green fluorescent protein (GFP) fused to synaptosome-associated protein of 25 kDa (SNAP-25) have been used to test the involvement of single amino acids in exocytotic function, overcoming some of the limitations of studies based on Botulinum neurotoxin cleavage, as this occurs at defined sites of the protein. Constructs containing either the whole SNAP-25 polypeptide or several deleted forms lacking its C-terminal domain were heavily overexpressed in transfected cells. All GFP-fusions were located in both the cytoplasm and the plasma membrane. Although a construct containing complete SNAP-25 sustained normal secretion, removal of four or more amino acids of its C terminus greatly altered the overall rate and extent of exocytosis. Further mutational analysis proved that Leu203, the fourth residue from the C terminus, is critical for secretion. Kinetics of single granule fusions from cells expressing truncated forms showed slow onset and decay times when compared with control cells expressing full SNAP-25. Thus, these data provide direct evidence for the involvement of a specific residue of SNAP-25 in exocytosis and show that overexpression of GFP-SNAP contructs combined with single vesicle fusion measurements constitutes a powerful approach to dissect the structural elements playing a role in individual steps of the exocytotic cascade.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.