Publication for Snap23 and Vamp3

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Snap23	synaptosomal-associated protein 23	20619			[link]
mmu	Vamp3	vesicle-associated membrane protein 3	22319

Pubmed ID	Priority	Text
16330817	0.98	cellubrevin, SNAP-23 and SNAP-25, and syntaxin-2 and syntaxin-4, as well as VAMP-3 and VAMP-8, and interference with their function abolishes exocytosis from platelet alpha, dense, and lysosomal granules.
20148679	0.98	cellubrevin ] and SNAP-23, and ancillary proteins to this complex, such as Munc 18, complexin 2, and synaptotagmin IV.
22587993	0.98	SNAP-23, Syntaxin-4, VAMP-1, VAMP-2 and VAMP-3, as well as NSF and its co-factor alpha-SNAP, the calcium sensor synaptogamin, and the GTPases Rab8 and Rab4.
27319345	0.98	SNAP23 is stabilized by SNARE complexes (SNAP-23/Syntaxin4/Vamp-3) promoting fusion between ERCs and phagosomes.
28524818	0.98	SNAP23 was recently shown to be phosphorylated in an IkappaB-kinase two dependent fashion upon stimulation of mouse dendritic cells with LPS and this mediates the delivery of major histocompatibility complex (MHC) class I from recycling endosomes to phagosomes, presumably via Stx4 and VAMP3 or VAMP8.
29910809	0.98	SNAP-23 in non-neuronal cells) and one v-SNARE such as VAMP3 allows the docking and priming of the vesicle, which fuses with the plasma membrane in the presence of high Ca2+.
31712554	0.98	SNAP23 and VAMP3, but not SNAP29 (Fig. 6c; Supplementary Fig. 6A).
31835680	0.98	vesicle associated membrane protein (VAMP)-3/Snap23/syntaxin 4-dependent release of EVs into the extracellular environment.
24431989	0.97	VAMP3 pairs with syntaxin-4 and SNAP23, while VAMP7 binds to syntaxin-3/SNAP23, equivalent to polarized epithelial cells, where the same complexes control fusion of apical and basolateral cargos, respectively (Carmosino et al.,).
	0.94	VAMP3 (red) mediates fusion of recycling endosome (RE)-derived vesicles with the plasma membrane, where Syntaxin 4 (Stx4) and SNAP23 act as cognate target-SNARES (orange).
31052241	0.97	VAMP3) fuse with the astrocyte cell membrane fusion proteins (syntaxin and soluble N-ethylmaleimide-sensitive factor attachment protein 23 (SNAP23)), resulting in glutamate release from the vesicles into the extracellular space.
	0.97	VAMP3) was significantly upregulated in Nlrx1-/- astrocytes relative to WT (Figure 3A), while no significant change was observed in the mRNA expression of the cell membrane fusion proteins (Syntaxin 1a and SNAP23) (Figure 3B) or the proteins upstream of the Ca2+ release (V-ATPase d2, VGLUT1, and VGLUT2) (Figure 3C).
21708949	0.97	VAMP3, syntaxin 3 and 4, and SNAP-23.
31920989	0.96	VAMP3, SNAP23, Munc18) expression or localization with skeletal muscle and adipose insulin resistance.
22251135	0.95	cellubrevin located at vesicular membrane and ii) the binary cis complex pre-formed at the plasma membrane and composed of syntaxin (shown in an open form) and SNAP-23.
22639011	0.95	cellubrevin, and SNAP (synaptosomal-associated protein)-23 instead of SNAP-25 (Hepp et al.,; Parpura et al.,).
31906003	0.95	SNAP-23 and VAMP3.
21880114	0.94	SNAP-23, Syntaxin 4, VAMP-2, VAMP-3, VAMP-7 and VAMP-8 in mast cell degranulation in studies using streptolysin-O-permeabilized cells and inhibitory recombinant SNARE proteins, SNARE neutralizing antibodies; overexpression studies, RNA interference methods and SNARE-deficient mice.
23087210	0.93	SNAP-23 (Qbc-SNARE protein) interacts with plasmalemmal SNARE proteins, such as syntaxins 2, 3, 4, and 11 (Qa-SNARE proteins) and VAMP5 (R-SNARE protein; Figure S8A), and with endocytic SNARE proteins, such as VAMP3, VAMP7, and VAMP8 (R-SNARE proteins) and syntaxins 7 and 13 (Qa-SNARE proteins), to form a SNARE complex.
22069605	0.92	cellubrevin/VAMP-3, syntaxin 2, syntaxin 3, and the murine SNAP-23 proved to be substrates for the respective CNT serotypes (reviewed in).
29623913	0.92	SNAP23, and VAMP3 (cellubrevin) (Schubert et al., 2011).
25501368	0.89	SNAP23, and whereas many studies identify VAMP2 as the v-SNARE, others suggest that either VAMP3 or VAMP8 may also fulfil this role.
24162806	0.79	VAMP 3, syntaxin 1B and SNAP 23) leading to the stable docking between the plasma membrane and outer acrosomal membrane , followed by disassembly of this docking complex and assembly of the fusion-driving SNARE complex (syntaxin 3, SNAP 23 and VAMP 2) with an additional interacting protein (complexin 2); changes in surface glycoconjugates; increases and decrease in phosphorylated proteins; increases in intracellular calcium; activation of phospholipase A2; and changes in the expression and localization of actin.