Recombinant Mouse Synaptosomal-associated protein 23 (Snap23)

1. PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23. PMID: 28067230
2. These results demonstrate opposing roles for SNAP23 in the secretion mechanisms of the endocrine and exocrine pancreas. PMID: 27697926
3. SNAP23 is selectively expressed in airway secretory cells and mediates baseline and stimulated mucin secretion. PMID: 26182382
4. these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis. PMID: 26266817
5. Data indicate that acute depletion of synaptosomal-associated protein 23 (SNAP-23) in fibroblasts leads to rapid apoptotic cell death. PMID: 25706117
6. Use of neurons from double-knock-out (SNAP-25, synaptotagmin-7) mice in combination with viral transduction showed that SNAP-23-driven release is triggered by endogenous synaptotagmin-7 PMID: 25422940
7. Results suggest that Plin2 inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets. PMID: 24040030
8. morphine suppresses TLR4-induced TNF release in mast cells, preventing the IKK-dependent phosphorylation of SNAP-23, which is necessary for TNF exocytosis, and this inhibition correlates with the formation of a beta-arrestin-2/TRAF6 complex PMID: 23960234
9. We report the regulation of platelet secretion via phosphorylation of SNAP-23 at Ser95. PMID: 23613522
10. Results suggest that phagosomal SNAP-23 is one of the key players regulating the phagosomal environment in macrophages. PMID: 23087210
11. We concluded that the SNARE protein SNAP23 mediates cAMP-stimulated renin release. PMID: 23269646
12. 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. PMID: 21656854
13. By altering the levels of individual components of the VAMP3/Stx4/SNAP23 complex we show here that this SNARE complex regulates efficient macrophage adhesion, spreading and migration on fibronectin. PMID: 21586284
14. These data reveal a critical role for SNAP-23 during embryogenesis. PMID: 21479242
15. SNAP-23, but not SNAP-25, is important for the functional regulation of postsynaptic glutamate receptors. PMID: 20118925
16. the majority of SNAP-23 is associated with non-caveolar, cholesterol-rich lipid rafts PMID: 12376543
17. Palmitoylated peptides from the cysteine-rich domain of this protein cause membrane fusion depending on peptide length, position of cysteinees, and extent of palmitoylation. PMID: 12551899
18. Interacts with tomosyn and plays a role in insulin-stimulated GLUT4 translocation. PMID: 12832401
19. Overexpression of SNAP-23 resulted in a distinct phenotype; SNAP-23 did not support a standing pool of primed secretory vesicles. PMID: 12859899
20. different raft-targeting signals within SNAP-25 and SNAP-23 are likely important for fine-tuning the exocytic pathways in which these proteins operate PMID: 15542596
21. addition of PIP2 to Stx4/SNAP23 vesicles inhibited the fusion reaction, and its addition to VAMP2 vesicles was stimulatory PMID: 17001002
22. These results suggest that IKK2 phosphorylation of SNAP-23 leads to degranulation and anaphylactic reactions. PMID: 18692471
23. Data show that in VAMP-8-deficient cells constitutive vesicular trafficking mechanisms are perturbed as indicated by increased SNARE complex formation between VAMP-3 and SNAP-23. PMID: 19274433
24. ablation of SNAP23 using siRNA reduced complex formation and beta oxidation, which suggests that the lipid droplets-mitochondria complex is functional in the cell. PMID: 19524684

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KEGG: mmu:20619

STRING: 10090.ENSMUSP00000112138

UniGene: Mm.245715