| 1996 |
SNAP-23 was identified as a 23-kDa protein from human B lymphocytes that binds to multiple syntaxins and synaptobrevins/VAMPs in vitro, establishing it as a ubiquitously expressed homolog of SNAP-25 and component of the t-SNARE complex in non-neuronal cells. |
Yeast two-hybrid screen, in vitro binding assays |
The Journal of biological chemistry |
High |
8663154
|
| 1997 |
SNAP-23 is palmitoylated in vivo on cysteine residues in a central palmitoylation domain, and the extent of palmitoylation correlates with its ability to bind syntaxin in vivo. SNAP-23 is less palmitoylated than SNAP-25. |
Metabolic labeling with [3H]palmitate, in vivo binding studies |
Biochemical and biophysical research communications |
High |
10329400
|
| 1997 |
SNAP-23 is resistant to cleavage by botulinum neurotoxin E (BoNT/E), unlike SNAP-25, and can functionally replace SNAP-25 to reconstitute insulin secretion in BoNT/E-treated HIT cells when overexpressed. |
BoNT/E cleavage assay, transfection rescue experiment in HIT cells |
The Journal of biological chemistry |
High |
9407084
|
| 1997 |
Munc18c inhibits the binding of SNAP-23 to syntaxin 4 in a concentration-dependent manner, as shown in COS cell co-expression experiments. |
Co-expression in COS cells, co-immunoprecipitation |
Biochemical and biophysical research communications |
Medium |
9168999
|
| 1997 |
SNAP-23 localizes predominantly to the plasma membrane in 3T3-L1 adipocytes and is membrane-bound across multiple non-neuronal tissues, with the majority associated with plasma membranes in subcellular fractionation. |
Subcellular fractionation, immunoblotting, immunofluorescence |
Biochemical and biophysical research communications |
High |
9020061
|
| 1998 |
SNAP-23 forms binary, saturable interactions with syntaxin-4 and VAMP-2 in vitro. PKA phosphorylation of syntaxin-4 disrupts its binding to SNAP-23, whereas SNAP-23 does not potentiate VAMP-2 binding to syntaxin-4 (unlike neuronal SNAP-25). |
In vitro binding assays, phosphorylation by exogenous kinases (PKA, CKII, PKC) with binding readout |
Biochemistry |
High |
9693005
|
| 1998 |
In response to stimulation, SNAP-23 relocates from plasma membrane lamellipodia-like projections to granule membranes in mast cells, and this relocation is required for compound exocytosis (granule-plasma membrane and granule-granule fusions). |
Permeabilized mast cell exocytosis assay, immunofluorescence, functional antibody inhibition |
Cell |
High |
9727496
|
| 1998 |
SNAP-23 is required for transferrin recycling in MDCK cells: it is cleaved by BoNT/E in these cells, and addition of exogenous SNAP-23 or anti-SNAP-23 antibodies both inhibit ligand recycling in permeabilized cells. |
Streptolysin O-permeabilized MDCK cell reconstitution assay, BoNT/E cleavage, antibody inhibition |
The Journal of biological chemistry |
High |
9651373
|
| 1998 |
SNAP-23 colocalizes with aquaporin-2 in collecting duct vesicles of rat kidney, and synaptobrevin-2 (VAMP-2) is also present in these AQP2-bearing vesicles, consistent with a role in vasopressin-regulated AQP2 trafficking. |
Subcellular fractionation, immunoisolation of AQP2-bearing vesicles, immunoblotting |
The American journal of physiology |
Medium |
9815132
|
| 1999 |
SNAP-23 forms 20S SNARE complexes with syntaxin 4 and VAMP2/3 in rat adipose cell membranes with recombinant alpha-SNAP and NSF, and co-immunoprecipitates with syntaxin 4 in plasma membranes; insulin stimulation does not alter the SNAP-23/syntaxin 4 complex stoichiometry. |
Co-immunoprecipitation, 20S SNARE complex reconstitution with recombinant proteins |
The Biochemical journal |
High |
10051443
|
| 1999 |
Syntaxin 11, identified by yeast two-hybrid screen using SNAP-23 as bait, binds SNAP-23 and VAMP in vitro and forms a complex with SNAP-23 in transfected HeLa cells and native B lymphocytes. Syntaxin 11 colocalizes with mannose 6-phosphate receptor on late endosomes and the trans-Golgi network. |
Yeast two-hybrid, in vitro binding, co-immunoprecipitation in transfected and native cells, immunofluorescence |
Journal of cell science |
High |
10036234
|
| 1999 |
SNAP-23 is required for insulin-stimulated GLUT4 translocation to the plasma membrane: microinjection of anti-SNAP-23 C-terminal antibody inhibited GLUT4 membrane incorporation, while recombinant SNAP-23 enhanced the insulin effect. |
Microinjection of antibody and recombinant protein, permeabilized cell glucose transport assay |
The American journal of physiology |
High |
10329959
|
| 1999 |
A novel kinase SNAK specifically phosphorylates SNAP-23 in vivo; only unassembled SNAP-23 (not in t-SNARE complexes) is phosphorylated, phosphorylated SNAP-23 resides in the cytosol, and SNAK co-expression enhances SNAP-23 stability and augments syntaxin assembly. |
In vivo phosphorylation assay, co-immunoprecipitation, co-expression studies |
Molecular biology of the cell |
High |
10588641
|
| 1999 |
Botulinum toxin B (which cleaves cellubrevin/synaptobrevin) blocks insulin-stimulated GLUT4 translocation and glucose uptake in 3T3-L1 adipocytes; BoNT/A failed to cleave SNAP-23 and did not block glucose uptake, implicating cellubrevin rather than SNAP-23 proteolysis in one pathway of GLUT4 fusion. |
Toxin treatment of 3T3-L1 adipocytes, GLUT4 translocation assay, immunoblotting |
Biochemistry |
Medium |
9153412
|
| 1999 |
Protein kinase B (PKB/Akt) stimulates GLUT4 translocation via a pathway involving SNAP-23 and synaptobrevin-2/cellubrevin; Clostridium botulinum toxin E (which cleaves SNAP-23) abolished PKB-DD-stimulated GLUT4 translocation but not insulin-stimulated GLUT1 or transferrin receptor translocation. |
Microinjection of botulinum toxins B and E into 3T3-L1 adipocytes, GLUT4 translocation assay |
The Journal of biological chemistry |
High |
10497159
|
| 1999 |
SNAP-23 associates with vimentin intermediate filaments in a Triton X-100-insoluble fraction in fibroblasts. Upon NEM treatment, SNAP-23 dissociates from vimentin and forms a complex with syntaxin 4, suggesting vimentin-associated SNAP-23 serves as a reservoir for the plasma membrane fusion machinery. |
Detergent fractionation, co-immunoprecipitation, NEM treatment |
Molecular biology of the cell |
Medium |
11029050
|
| 2000 |
SNAP-23 and syntaxin 4 are required for platelet alpha-granule release: they form a SDS-resistant heterotrimeric complex with VAMP that disassembles upon platelet activation, and antibodies to syntaxin 4 inhibited ~75% of Ca2+-induced alpha-granule release. |
Streptolysin O-permeabilized platelet exocytosis assay, co-immunoprecipitation, antibody inhibition, tetanus toxin cleavage |
The Journal of biological chemistry |
High |
9891020
|
| 2000 |
SNAP-23 antibodies and C-terminal SNAP-23 peptide inhibit dense core granule release from platelets; SNAP-23 forms a complex in vivo with syntaxin 2, and anti-syntaxin 2 antibody also blocked dense core granule release. |
Streptolysin O-permeabilized platelet exocytosis assay, antibody/peptide inhibition, co-immunoprecipitation |
Blood |
High |
10648404
|
| 2000 |
SNAP-23 mediates specific (CD67-enriched) granule secretion in human neutrophils but has little effect on azurophilic (CD63-enriched) granule exocytosis; SNAP-23 translocates to the cell surface upon activation and interacts with syntaxin 6 in vitro and in vivo, with interaction dramatically increased upon activation. |
Electropermeabilized neutrophil exocytosis assay, antibody inhibition, in vitro binding, co-immunoprecipitation |
Blood |
High |
11001914
|
| 2000 |
SNAP-23 wild-type promotes the interaction between syntaxin 4 and VAMP2 both in vitro and in vivo; a C-terminal deletion mutant SNAP-23-ΔC8 that binds syntaxin 4 but not VAMP2 failed to mediate this interaction and inhibited insulin-induced GLUT4 but not GLUT1 translocation when overexpressed in adipocytes. |
In vitro binding, co-immunoprecipitation, adenovirus-mediated overexpression in 3T3-L1 adipocytes, GLUT4 translocation assay |
The Journal of biological chemistry |
High |
10713150
|
| 2000 |
Platelet lysosome exocytosis requires both syntaxin 2 and syntaxin 4 together with SNAP-23 as t-SNARE components, in addition to NSF and ATP; these localize to granule membranes and open canalicular system respectively. |
Streptolysin O-permeabilized platelet exocytosis assay, antibody inhibition, localization studies |
Blood |
High |
10961877
|
| 2001 |
The C-terminal domain of SNAP-23 (encoded by the last exon, 23 amino acids) is required for binding to VAMP but not syntaxin; overexpression of the carboxyl-terminal VAMP-binding mutant failed to enhance mast cell exocytosis, while wild-type SNAP-23 significantly enhanced it. |
Deletion mutagenesis, in vitro binding assays, overexpression in RBL mast cells with exocytosis assay |
The Journal of biological chemistry |
High |
11350976
|
| 2001 |
SNAP-23 is required for regulated surfactant secretion in alveolar type II cells; SNAP-23 and syntaxin 2 both associate with plasma membrane and lamellar bodies, and peptides or antibodies targeting either protein inhibit Ca2+- and GTPγS-stimulated surfactant secretion from permeabilized cells. |
Antisense oligonucleotide knockdown, peptide/antibody inhibition in permeabilized type II cells, subcellular fractionation |
Biochemistry |
High |
15035620
|
| 2001 |
SNAP-23 mediates H+-ATPase exocytosis to the apical membrane in inner medullary collecting duct (IMCD) cells; botulinum toxin A or E cleaves SNAP-23, reduces 20S SNARE complex formation, impairs H+-ATPase apical translocation by ~52%, and reduces H+ secretion by ~77%. |
Botulinum toxin cleavage, SNARE complex immunoprecipitation, H+-ATPase translocation and H+ secretion assays |
American journal of physiology. Cell physiology |
High |
11245593
|
| 2002 |
Calpain specifically cleaves SNAP-23 (but not syntaxins 2 and 4 or alpha-SNAP) in activated platelets in a Ca2+-dependent and time-dependent manner; cleavage site is in the C-terminal third of the molecule; this occurs after granule release and may affect granule membrane exteriorization. |
In vitro calpain cleavage assay in permeabilized platelets, calpain inhibitors (calpeptin, calpastatin), Ca2+ dose-response |
The Journal of biological chemistry |
High |
12121992
|
| 2002 |
SNAP-23 localizes predominantly to the plasma membrane in resting platelets (by immunonanogold electron microscopy), whereas human cellubrevin localizes ~80% to granule membranes and syntaxin 2 is distributed among alpha-granules, OCS, and plasma membrane. |
Pre-embedding immunonanogold electron microscopy, immunoblotting of subcellular fractions |
Blood |
High |
12010801
|
| 2002 |
Kinesin heavy chain (residues 814–907) binds to SNAP-23 and SNAP-25 via coiled-coil interactions; the minimal SNAP23-binding region on kinesin is its cargo-binding domain, and a complex of kinesin heavy and light chains retains the ability to interact with SNAP-23. |
Yeast two-hybrid, in vitro and in vivo binding assays |
Biochemistry |
Medium |
12475239
|
| 2003 |
SNAP-23 is phosphorylated in thrombin-activated platelets predominantly on serine residues via a PKC mechanism; phosphorylation at Ser23/Thr24 inhibits syntaxin 4 interactions; SNAP-23 phosphorylation kinetics parallel or precede granule secretion. |
32P metabolic labeling, tryptic peptide mapping, mass spectrometry, PKC phosphorylation of recombinant SNAP-23, phosphomimetic mutant binding assays |
The Journal of biological chemistry |
High |
12930825
|
| 2003 |
Snapin interacts with SNAP-23 (the ubiquitous SNAP-25 homolog) via its C-terminal helical domain and forms a ternary complex with SNAP-23 and syntaxin 4 in non-neuronal cells. |
Protein-protein interaction assays, deletion mapping, subcellular localization with GFP fusion, co-immunoprecipitation |
The Biochemical journal |
Medium |
12877659
|
| 2003 |
b-Tomosyn forms a high affinity ternary complex with Syntaxin4 and SNAP23 that is competitively inhibited by VAMP-2; overexpression of Tomosyn in 3T3-L1 adipocytes inhibited GFP-GLUT4 translocation to the plasma membrane. |
In vitro binding assay, yeast two-hybrid, 3T3-L1 adipocyte overexpression with GLUT4-GFP translocation assay |
The Journal of biological chemistry |
Medium |
12832401
|
| 2004 |
SNAP-23 phosphorylation at Ser95 and Ser120 is induced during mast cell degranulation and mouse platelet activation; overexpression of phosphorylation-deficient SNAP-23 mutants inhibits exocytosis; essentially all SNAP-23 in SNARE complexes (with syntaxin 4 and VAMP-2) is phosphorylated after stimulation. |
32P metabolic labeling, site-directed mutagenesis, overexpression in RBL mast cells, co-immunoprecipitation |
The Journal of biological chemistry |
High |
15611044
|
| 2004 |
SNAP-23 and SNAP-25 display different affinities for lipid raft microdomains: SNAP-23 (~54% raft-associated) is ~3-fold more enriched in rafts than SNAP-25 (~20%), due to substitution of a conserved phenylalanine in SNAP-25 with a cysteine in SNAP-23 that provides an additional palmitoylation site enhancing raft association. |
Detergent-resistant membrane isolation, site-directed mutagenesis of cysteine/phenylalanine residues |
The Journal of biological chemistry |
High |
15542596
|
| 2004 |
SNAP-23 mediates granule docking at low Ca2+ (100 nM), whereas SNAP-25 mediates docking at high Ca2+ (1 μM), by interacting with different synaptotagmin family members; in intact endocrine cells, exogenous SNAP-23 increases basal (unstimulated) hormone secretion. |
In vitro granule docking assay with defined Ca2+ levels, overexpression in intact endocrine cells |
Molecular biology of the cell |
Medium |
14742706
|
| 2005 |
SNAP-23 directly interacts with L-type Ca2+ channels in pancreatic acinar cells, demonstrated by yeast two-hybrid and immunoanalysis. |
Yeast two-hybrid, co-immunoprecipitation/immunoanalysis |
Journal of cellular and molecular medicine |
Low |
15963257
|
| 2005 |
SNAP-23 and syntaxin-4 form cholesterol-dependent clusters on the endothelial basolateral plasma membrane, and ~50% of caveolae co-localize with these t-SNARE clusters during fusion, indicating these clusters are fusion sites for caveolar exocytosis. |
Cell-free caveolar fusion assay with plasma membrane sheets, correlative fluorescence microscopy and immunonanogold electron microscopy |
The Journal of biological chemistry |
High |
16118213
|
| 2007 |
Annexin A2 binds SNAP-23 in a Ca2+-dependent manner via the cysteine-rich region (CRR) of SNAP-23; mutations of cysteines in the CRR dramatically reduced binding; anti-SNAP-23 antibody inhibited annexin A2-mediated fusion of lamellar bodies with the plasma membrane in alveolar type II cells. |
GST pulldown, co-immunoprecipitation, deletion/mutation analysis, in vitro fusion assay with inhibitory antibody |
American journal of respiratory cell and molecular biology |
High |
17575076
|
| 2007 |
SNAP-23 and syntaxin-2 are expressed on the extracellular surface of the platelet plasma membrane; acyl-protein thioesterase 1 and botulinum toxin C light chain release SNAP-23 and syntaxin-2 respectively from intact platelet surfaces, and extracellular SNAP-23 retains the ability to bind syntaxin-2. |
Immunonanogold electron microscopy, flow cytometry of intact platelets, selective enzymatic release (APT1, BoNT/C), co-immunoprecipitation of released proteins |
Blood |
Medium |
17485553
|
| 2008 |
IKK2 (IκB kinase 2) phosphorylates SNAP-23 in mast cells upon FcεRI stimulation; IKK2-deficient mast cells show impaired IgE-mediated degranulation, and ectopic expression of a phospho-mimetic SNAP-23 mutant partially rescues this defect. This function is NF-κB-independent. |
IKK2 knockout mice, in vitro degranulation assay, phospho-mimetic mutant rescue, in vivo anaphylaxis model |
Cell |
High |
18692471
|
| 2009 |
SNAP-23 mediates lipid droplet–mitochondria complex formation in NIH 3T3 fibroblasts; siRNA ablation of SNAP23 reduced LD-mitochondria complex formation and beta-oxidation in an in vitro system of purified LD and mitochondria. |
siRNA knockdown, confocal and electron microscopy, in vitro LD-mitochondria interaction assay, beta-oxidation measurement |
Cell biology international |
Medium |
19524684
|
| 2009 |
SNAP-23 in the SNARE complex containing SNAP-23A has less than half the stability of the complex containing SNAP-25B, as measured by single-molecule force spectroscopy; both create a local interaction at the ionic layer cuffing syntaxin 1A and synaptobrevin 2, positioning vesicles at ~13 nm from the plasma membrane. |
Single molecule force spectroscopy (AFM), ternary SNARE complex reconstitution |
The Journal of physiology |
Medium |
19273577
|
| 2009 |
VAMP3, SNAP23, and syntaxin-13 colocalize with MMP2 and MMP9; dominant-negative SNARE mutants, RNAi, or tetanus toxin targeting these SNAREs impaired MMP secretion, MT1-MMP cell surface delivery, gelatin substrate degradation, and cell invasion. |
Dominant-negative SNARE mutants, RNAi, tetanus toxin, gelatin degradation assay, invasion assay |
Journal of cell science |
High |
19910495
|
| 2009 |
SNAP-23 has punctate perinuclear localization overlapping with endosomal/transferrin receptor compartments in HepG2 and HT4 cells, distinct from the predominant plasma membrane pool, and redistributes to the apical domain as HepG2 cells polarize. |
Immunofluorescence, GFP-SNAP-23 expression, subcellular localization in polarizing cells |
Biochemical and biophysical research communications |
Medium |
10049710
|
| 2010 |
SNAP-23 is enriched in dendritic spines and colocalizes with postsynaptic density components in neurons; loss of SNAP-23 (by KO mice or shRNA) markedly decreases NMDA receptor surface expression and NMDA receptor currents, whereas SNAP-25 loss does not affect postsynaptic NMDA receptors. |
Conditional knockout mice, shRNA knockdown, immunofluorescence, electrophysiology, surface receptor assay |
Nature neuroscience |
High |
20118925
|
| 2011 |
SNAP-23 deletion results in pre-implantation embryonic lethality in mice; Snap23-null blastocysts die prior to implantation at E3.5, demonstrating SNAP-23 is essential for early embryogenesis. |
Homologous recombination to generate Snap23-null mice, analysis of pre-implantation embryos |
PloS one |
High |
21479242
|
| 2011 |
Conditional deletion of SNAP-23 in CD19-Cre mice prevents B lymphocyte development; deletion using T lymphocyte-specific Cre mice prevents T lymphocyte development; acute depletion of SNAP-23 in fibroblasts leads to rapid apoptotic cell death. |
Conditional Cre-lox knockout mice, lymphocyte development assays, fibroblast apoptosis assay |
PloS one |
High |
25706117
|
| 2012 |
SNAP-23 overexpression enhances Fc receptor-mediated phagocytosis in macrophages and promotes ROS production and acidification in phagosomes; SNAP-23 knockdown delays phagosome maturation and reduces uptake. SNAP-23 undergoes conformational change (increased FRET) on phagosomes specifically when VAMP7 is coexpressed. |
Stable cell line overexpression, siRNA knockdown, FRET probe, phagosome isolation, ROS and pH measurements |
Molecular biology of the cell |
High |
23087210
|
| 2013 |
IKKβ phosphorylation of SNAP-23 at Ser95 controls platelet secretion; IKKβ inhibition or platelet-specific IKKβ knockout blocked SNAP-23 phosphorylation, platelet secretion, and SNARE complex formation; SNAP-23 phosphorylation enhanced membrane fusion of SNARE-containing proteoliposomes. |
IKKβ inhibitors, platelet-specific IKKβ-flox/flox × PF4-Cre mice, proteoliposome fusion assay, SNARE complex co-IP |
Blood |
High |
23613522
|
| 2013 |
IKK-dependent phosphorylation of SNAP-23 is required for LPS-induced TNF secretion in mast cells; morphine prevents this by blocking IKK activation via a β-arrestin-2/TRAF6 complex, and SNAP-23 forms a complex with IKK in LPS-activated BMMCs. |
Bone marrow-derived mast cell activation assay, phosphorylation assays, co-immunoprecipitation, siRNA knockdown, pharmacological inhibition |
Journal of immunology |
Medium |
23960234
|
| 2014 |
During invadopodium formation in MDA-MB-231 breast cancer cells, SNAP23, Syntaxin4, and VAMP7 form a ternary complex (detected by co-IP) that is required for MT1-MMP trafficking to invadopodia, ECM degradation, and cell invasion; increased SNAP23-Stx4-VAMP7 interaction correlates with decreased Syntaxin4 phosphorylation. |
Co-immunoprecipitation, dominant-negative SNARE perturbation, MT1-MMP localization assay, gelatin degradation, invasion assay |
Molecular biology of the cell |
High |
24807903
|
| 2014 |
When SNAP-23 replaces SNAP-25 in hippocampal neurons, release becomes asynchronous and is triggered by endogenous synaptotagmin-7 (a plasma membrane Ca2+ sensor); SNAP-23-driven release is more asynchronous and has higher spontaneous release rates than SNAP-25-driven release. |
Viral transduction into SNAP-25/synaptotagmin-7 double-KO mouse autaptic neurons, electrophysiology, pHluorin imaging |
PloS one |
High |
25422940
|
| 2015 |
SNAP23 is the predominant SNAP isoform in endothelial cells and localizes to the plasma membrane; SNAP23 knockdown decreased endothelial exocytosis of von Willebrand Factor and SNAP23 forms complexes with other known endothelial SNARE molecules. |
siRNA knockdown, VWF exocytosis assay, co-immunoprecipitation, immunofluorescence localization |
PloS one |
Medium |
26266817
|
| 2015 |
SNAP23 is selectively expressed in airway secretory (goblet) cells and is required for stimulated mucin secretion; heterozygous SNAP23 knockout mice show impaired acute stimulated mucin release from perfused tracheas. |
Immunohistochemistry/FACS for cell-type selectivity, heterozygous Snap23 KO mouse trachea perfusion assay, static imaging assay |
Bioscience reports |
Medium |
26182382
|
| 2015 |
BoNT/A resistance of SNAP-23 is conferred by 10 specific residues differing from SNAP-25; replacing these with SNAP-25 counterparts renders SNAP-23 cleavable by BoNT/A; conversely, transferring any of these SNAP-23 residues to SNAP-25 drastically decreases BoNT/A cleavability. |
Site-directed mutagenesis, BoNT/A cleavage assay, yeast-based screening, molecular dynamics simulation |
Journal of molecular biology |
High |
26523682
|
| 2015 |
SNAP23 and VAMP2 mediate the fusion of transferrin receptor-containing recycling vesicles with the plasma membrane downstream of the exocyst complex; depletion of SNAP23 and/or SNAP25 suppresses recycling vesicle fusion, causing accumulation at the cell periphery. |
siRNA depletion, transferrin recycling assay, immunofluorescence colocalization |
Biology open |
Medium |
26092867
|
| 2016 |
Loss of SNAP-23 in exocrine pancreas decreases stimulated granule fusion, while loss in endocrine pancreas increases granule fusion; MF286, a small molecule identified to bind specifically to SNAP23, promotes insulin secretion in mice. |
Pancreas-specific SNAP23 conditional KO mice, single granule imaging, small molecule screen and binding assay, in vivo insulin secretion assay |
The Journal of cell biology |
High |
27697926
|
| 2016 |
Septin 7 forms a complex with NM-IIA and SNAP23; insulin decreases septin 7 and increases NM-IIA activity (myosin regulatory light chain phosphorylation) in the SNAP23 complex; septin 7 knockdown increases NM-IIA activity in the complex; NM-IIA activity in the SNAP23 complex promotes GSV docking/fusion with the plasma membrane in podocytes. |
Co-immunoprecipitation, siRNA knockdown, myosin light chain phosphorylation assay, glucose uptake assay |
Experimental cell research |
Medium |
28011197
|
| 2017 |
Electrostatic anchoring by basic amino acids in the cysteine-rich region of SNAP-23 (and SNAP-25) mediates initial plasma membrane targeting through interaction with acidic lipids (phosphoinositides), prior to palmitoylation and stable membrane attachment. |
Site-directed mutagenesis of basic residues, liposome binding reconstitution assay, live cell imaging in neuroendocrine cells |
eLife |
High |
28240595
|
| 2017 |
Rab5 is required for SNAP23 association with secretory granules in stimulated mast cells, and is pivotal for SNAP23-mediated homotypic granule-granule fusion (compound exocytosis); Rab5 silencing shifts secretion from compound to full (single granule) exocytosis mode. |
Rab5 siRNA silencing, live cell imaging, immunofluorescence, IKKβ2 inhibition |
Scientific reports |
Medium |
29127297
|
| 2017 |
Phosphorylation at Thr102 of SNAP-23 (basal site) is required for initial plasma membrane association; induced phosphorylation at Ser95 and Ser120 promotes SNAP-23 internal membrane (granule membrane) association during mast cell exocytosis. |
GFP-SNAP-23 phosphorylation site mutant overexpression in RBL mast cells, live fluorescence imaging |
Biology open |
Medium |
28784843
|
| 2018 |
Adipocyte-specific SNAP23 KO causes lipodystrophy through inhibition of ATG9-dependent (but ATG7-independent) macroautophagy, leading to failure of lysosomal BAX degradation, BAX activation, and apoptosis; BAX deficiency suppresses the lipodystrophic phenotype in SNAP23-KO mice. |
Adipocyte-specific conditional KO mice, BAX/ATG9/ATG7 co-deletion epistasis, lysosome inhibitor treatment, BAX colocalization with autophagic vacuoles |
The Journal of clinical investigation |
High |
30102258
|
| 2018 |
SNAP23 forms a complex with Kif5 kinesin and directly interacts with the carboxyl terminus of the mGlu1 receptor; disrupting or enhancing the SNAP23-Kif5 interaction alters mGlu1 receptor trafficking along microtubules and its cell surface expression in hippocampal neurons. |
Proteomics (co-IP/MS), direct interaction assay, recombination approach to alter SNAP23-Kif5 interaction, FRAC (fluorescence recovery after cleavage) imaging |
Journal of molecular cell biology |
Medium |
29762713
|
| 2019 |
SNAP23 is required for cortical granule exocytosis (regulated exocytosis) and for meiotic arrest in mouse oocytes; SNAP23 depletion (by Trim-away) causes premature meiotic resumption associated with loss of gap junction communication between oocyte and follicle cells. |
Trim-away protein depletion in oocytes, lectin staining/ZP2 cleavage for cortical granule exocytosis, meiotic arrest assay |
Biology of reproduction |
Medium |
31201423
|
| 2019 |
Syntaxin 11 cooperates with SNAP-23 to regulate stimulus-dependent transport of TLR4 to the plasma membrane in macrophages; stx11 or SNAP-23 knockdown impairs TLR4 replenishment after LPS stimulation; stx11 knockdown reduces the FRET efficiency of an intramolecular SNAP-23 FRET probe induced by LPS stimulation. |
siRNA knockdown, TLR4 surface expression assay, intramolecular FRET probe for SNAP-23 conformational state |
Molecular biology of the cell |
Medium |
30811271
|
| 2020 |
Pancreatic SNAP23 phosphorylation at Ser95/Ser120 (rat) or Ser120 (human) by IKKβ causes SNAP23 translocation from plasma membrane to autophagosomes where it binds the STX17 SNARE complex to regulate autophagosome-lysosome fusion; phosphorylation-disabled SNAP23 (S95A/S120A) cannot bind STX17; pancreatic SNAP23 knockdown impairs both STX4-driven basolateral exocytosis and STX17-driven autolysosome formation, protecting rats from pancreatitis. |
adenovirus-shRNA knockdown in rodent and human pancreatic slices and in vivo, phospho-mutant analysis, SNARE complex co-IP, in vitro pancreatitis model |
Autophagy |
High |
33213278
|
| 2020 |
SNAP23 depletion in β cells paradoxically increases biphasic insulin secretion and exocytosis of both predocked and newcomer granules; in the context of β cells, SNAP23 acts as an inhibitory/weak partial fusion agonist by competing with SNAP25 for binding to Ca2+ channels at granule fusion sites. |
β-cell-specific conditional KO in mice, human islet viral knockdown (including T2D patients), single granule imaging, Ca2+ channel binding assay |
JCI insight |
High |
32051343
|
| 2020 |
NEDD4 (an E3 ubiquitin ligase) binds SNAP23 and promotes its ubiquitin-mediated proteasomal degradation; BTX-A reduces SNAP23 expression by inhibiting IKKα/β phosphorylation and enhancing NEDD4-mediated ubiquitination of SNAP23. |
Co-immunoprecipitation of NEDD4-SNAP23, proteasome inhibitor rescue, IKKα/β phosphorylation assay |
Cell & bioscience |
Medium |
33298171
|
| 2021 |
Reduced O-GlcNAcylation of SNAP-23 (caused by OGT downregulation) promotes formation of the SNARE complex (SNAP-23/VAMP8/Stx4), enhancing exosome release and cisplatin efflux in ovarian cancer cells; O-GlcNAcylation of SNAP-23 is a negative regulator of SNARE complex assembly and exosome secretion. |
OGT knockdown/overexpression, O-GlcNAcylation site analysis, SNARE complex co-IP, exosome quantification, cisplatin efflux assay |
Cell death discovery |
Medium |
34001861
|
| 2022 |
ICAM-1 clustering in endothelial cells recruits SNAP23 (along with syntaxin-3 and -4) to mediate local release of endothelial chemokines (CXCL1/8/10); SNAP23 silencing shifts CTL transmigration from transcellular to paracellular route. |
siRNA silencing of SNAP23, immunofluorescence of ICAM-1/SNAP23 colocalization, T lymphocyte transmigration assay, chemokine release assay |
Cell reports |
Medium |
35045291
|