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Synaptosomal-associated protein 23

Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues. The protein encoded by this gene is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion. Two alternative transcript variants encoding different protein isoforms have been described for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: SNAP-25, VAMP2, syntaxin 4, CAN, Insulin
Papers using SNAP-23 antibodies
Roles for gliotransmission in the nervous system
Meldolesi Jacopo et al., In The Journal of Cell Biology, 2004
... from Thermo Fisher Scientific; anti-Rab3a, anti-Stx1a, anti-Syt1, anti-Syp, and anti-VAMP2 mAb’s and anti-Munc18, anti-Syt4, and anti-SNAP23 rabbit pAb’s were obtained from Synaptic Systems; anti-SNAP25 mAb was obtained ...
Papers on SNAP-23
Immunofluorescence microscopy of SNAP23 in human skeletal muscle reveals colocalization with plasma membrane, lipid droplets, and mitochondria.
Wagenmakers et al., Geelong, Australia. In Physiol Rep, Jan 2016
Synaptosomal-associated protein 23 (SNAP23) is a SNARE protein expressed abundantly in human skeletal muscle.
Urodynamic and Immunohistochemical Evaluation of Intravesical Botulinum Toxin A Delivery Using Low Energy Shock Wave.
Huang et al., T'ai-chung-shih, Taiwan. In J Urol, Jan 2016
BoNT-A plus LESW pretreated rats showed decrease on inflammatory reaction (p<0.05) and expresson of SNAP-23 (p<0.05),
Effects of immobilization and aerobic training on proteins related to intramuscular substrate storage and metabolism in young and older men.
Helge et al., Copenhagen, Denmark. In Eur J Appl Physiol, Jan 2016
The biopsies were analyzed for muscle substrates; muscle perilipin protein (PLIN), glycogen synthase (GS), synaptosomal-associated protein of 23 kDa (SNAP23) protein content, and muscle 3-hydroxyacyl-CoA dehydrogenase (HAD) activity RESULTS: The older men had higher intramuscular triglyceride (IMTG) (73 %) and Glycogen (16 %) levels compared to the young men, and IMTG tended to increase with immobilization.
Correction: SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor.
Lowenstein et al., In Plos One, Dec 2015
UNASSIGNED: [This corrects the article DOI: 10.1371/journal.pone.0118737.].
Identification of roles for the SNARE-associated protein, SNAP29, in mouse platelets.
Poole et al., Cambridge, United Kingdom. In Platelets, Dec 2015
These data suggest that SNAP29 contributes to the regulation of platelet α-granule secretion and thrombus stability, possibly partially masked by functional redundancy with other tSNAREs, such as SNAP23.
TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation.
Blander et al., New York City, United States. In Cell, 2014
While Rab11a activity stocks ERC stores with MHC-I, MyD88-dependent TLR signals drive IκB-kinase (IKK)2-mediated phosphorylation of phagosome-associated SNAP23.
Metabolism and insulin signaling in common metabolic disorders and inherited insulin resistance.
Højlund, Odense, Denmark. In Dan Med J, 2014
In type 2 diabetes an altered intracellular distribution of SNAP23 and impaired activation of RAC1 also seem to play a role for reduced insulin action on glucose transport.
The SNARE Sec22b has a non-fusogenic function in plasma membrane expansion.
Galli et al., Paris, France. In Nat Cell Biol, 2014
Sec22b forms a trans-SNARE complex with syntaxin1 that does not include SNAP23/25/29, and does not mediate fusion.
Regulation of the NADPH oxidase and associated ion fluxes during phagocytosis.
Dinauer et al., Genève, Switzerland. In Traffic, 2013
Novel elements regulating catalytic core trafficking include Rab27 and SNAP-23.
Regulated mucin secretion from airway epithelial cells.
Dickey et al., Raleigh, United States. In Front Endocrinol (lausanne), 2012
The core exocytic machinery is comprised of the SNARE proteins VAMP8, SNAP23, and an unknown Syntaxin protein, together with the scaffolding protein Munc18b.
Annexin A7 and SNAP23 interactions in alveolar type II cells and in vitro: a role for Ca(2+) and PKC.
Chander et al., Stony Brook, United States. In Biochim Biophys Acta, 2012
Annexin A7 may function in co-ordination with SNARE proteins and that protein kinase activation may be required for annexin A7 trafficking.
Critical roles of IĸB kinase subunits in mast cell degranulation.
Nakajima et al., Chiba, Japan. In Int Arch Allergy Immunol, 2011
Recently, we showed that IKK2 (also called IKKβ), a catalytic subunit of the IKK complex, induces immunoglobulin E-mediated degranulation in mast cells by phosphorylating SNAP-23, the target-membrane soluble N-ethylmaleimide-sensitive fusion factor attachment protein receptor (SNARE).
The formation of lipid droplets: possible role in the development of insulin resistance/type 2 diabetes.
Boström et al., Göteborg, Sweden. In Prostaglandins Leukot Essent Fatty Acids, 2011
The fusion is catalyzed by the SNARE proteins SNAP23, syntaxin-5 and VAMP4.
SNARE protein expression in synaptic terminals and astrocytes in the adult hippocampus: a comparative analysis.
Volterra et al., Lausanne, Switzerland. In Glia, 2011
SNAP23 display robust and ubiquitous pattern of expression in adult hippocampal astrocytes and are therefore likely to be molecularly associated in the core SNARE complex underlying regulated exocytosis in these cells.
SNAP-23 and syntaxin-3 are required for chemokine release by mature human mast cells.
Lorentz et al., Stuttgart, Germany. In Mol Immunol, 2011
STX-3 and SNAP-23 are crucial for the release of all chemokines in mature human mast cells
Synaptic vesicle-like lipidome of human cytomegalovirus virions reveals a role for SNARE machinery in virion egress.
Shenk et al., Princeton, United States. In Proc Natl Acad Sci U S A, 2011
Data show that knockdown of SNAP-23 inhibited the production of virus.
Granule exocytosis contributes to priming and activation of the human neutrophil respiratory burst.
McLeish et al., Louisville, United States. In J Immunol, 2011
Introduction of the SNARE domain of SNAP-23 into neutrophils as an HIV transactivator of transcription (TAT) fusion protein significantly inhibits exocytosis of neutrophil granule subsets without altering signal transduction pathway activation.
Phosphorylation of SNAP-23 by IkappaB kinase 2 regulates mast cell degranulation.
Verma et al., Los Angeles, United States. In Cell, 2008
These results suggest that IKK2 phosphorylation of SNAP-23 leads to degranulation and anaphylactic reactions.
SNARE proteins mediate fusion between cytosolic lipid droplets and are implicated in insulin sensitivity.
Olofsson et al., Göteborg, Sweden. In Nat Cell Biol, 2007
Here, we show that lipid droplets are associated with proteins involved in fusion processes in the cell: NSF (N-ethylmaleimide-sensitive-factor), alpha-SNAP (soluble NSF attachment protein) and the SNAREs (SNAP receptors), SNAP23 (synaptosomal-associated protein of 23 kDa), syntaxin-5 and VAMP4 (vesicle-associated membrane protein 4).
Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23.
Neher et al., Göttingen, Germany. In Cell, 2003
Overexpression of SNAP-23 resulted in a distinct phenotype; SNAP-23 did not support a standing pool of primed secretory vesicles.
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