ArticleThe Biochemical journal2005
Promiscuous interaction of SNAP-25 with all plasma membrane syntaxins in a neuroendocrine cell.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 46 citations in OpenAlex.
- SNARE complex assembly and disassembly dynamics in response to CaBiophysical journal · 2025Article
- Article
- SNAP-25, but not SNAP-23, is essential for photoreceptor development, survival, and function in mice.Communications biology · 2024Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- SNAP23 is required for constitutive and regulated exocytosis in mouse oocytes†.Biology of reproduction · 2019Article
- Phosphatidylinositol (4, 5)-bisphosphate targets double C2 domain protein B to the plasma membrane.Traffic (Copenhagen, Denmark) · 2017Article
- The influence of cell membrane and SNAP25 linker loop on the dynamics and unzipping of SNARE complex.PloS one · 2017Article
- Botulinum neurotoxin type C protease induces apoptosis in differentiated human neuroblastoma cells.Oncotarget · 2016Article
- Botulinum protease-cleaved SNARE fragments induce cytotoxicity in neuroblastoma cells.Journal of neurochemistry · 2014Article
- Stapling of the botulinum type A protease to growth factors and neuropeptides allows selective targeting of neuroendocrine cells.Journal of neurochemistry · 2013Article
- Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.Investigative ophthalmology & visual science · 2011Article
- Alpha-synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis.EMBO reports · 2010Article
- Detecting the conformation of individual proteins in live cells.Nature methods · 2010Article
- Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments.Journal of cell science · 2009Article
- Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport.Journal of cell science · 2008Article
- Flow cytometry-assisted purification and proteomic analysis of the corticotropes dense-core secretory granules.Proteomics · 2008Article
- Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes.The Journal of cell biology · 2008Article
- Mechanism of arachidonic acid action on syntaxin-Munc18.EMBO reports · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SNAP-25 (25 kDa synaptosome-associated protein) is found in cells that release neurotransmitters and hormones, and plays a central role in the fusion of secretory vesicles with the plasma membrane. SNAP-25 has been shown to interact specifically with syntaxin 1, a 35 kDa membrane protein, to mediate the fusion process. Here, we investigated whether other known syntaxin isoforms found at the plasma membrane can serve as binding partners for SNAP-25 in vivo. In our analysis, we employed rat phaeochromocytoma PC12 cells that are often used as a model of neuronal functions. We now show that these cells contain large amounts of SNAP-25, which interacts not only with syntaxin 1, but also with ubiquitous syntaxins 2, 3 and 4. The plasma membrane syntaxins appear to occupy complementary domains at the plasma membrane. In defined reactions, the ubiquitous plasma membrane syntaxin isoforms, when in binary complexes with SNAP-25, readily bound vesicular synaptobrevin to form SDS-resistant SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) complexes implicated in membrane fusion. However, vesicular synaptotagmin and cytosolic complexin, both implicated in the fusion process, exhibited differential ability to interact with the SNARE complexes formed by syntaxins 1-4, suggesting that the plasma membrane syntaxins may mediate vesicle fusion events with different properties.
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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.