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Results show that SNAP23 is phosphorylated by HOTAIR promoting the release of exosome from hepatocellular carcinoma cells.
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Rab5 is essential for FcepsilonRI-triggered association of the SNARE protein SNAP23 with the secretory granules.
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Data suggest that acylation of SNAP23 (synaptosome associated protein 23) and STX11 (syntaxin-11) regulates exocytosis in platelets; maintaining acylation states of SNAP23 and STX11 is important for platelet function.
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PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23.
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SNAP23 suppressed progression of cervical cancer and induced cell cycle G2/M arrest via upregulating p21(cip1) and downregulating CyclinB1
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Knockdown of VAMP3 and SNAP23 reduces endothelial secretion of miR-126-3p and miR-200a-3p, as well as the proliferation, migration, and suppression of contractile markers in smooth muscle cells caused by vascular endothelial cell-coculture.
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Study showed that SNAP23 was recruited to the close sites of lipid droplet (LD) in HCV-infected cells, implying that SNAP23 was required for HCV-induced LD enlargement and, HCV production.
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A novel regulatory mechanism for SNAP23-dependent mast cell activation of T. vaginalis-secreted LTB4 involving surface trafficking of BLT1.
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Study identified SNAP23 as a novel oncogene in Ovarian Cancer (OC). It is over-expressed in OC and could promote the proliferation, migration and invasion of OC in vitro.
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Localization of SNAP23 was found in plasma membrane, lipid droplets and mitochondria of skeletal muscle.
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these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis.
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Increased level of SNAP23-Syntaxin4-VAMP7 interaction correlates with decreased Syntaxin4 phosphorylation and trafficking of MT1-MMP to invadopodia during cellular invasion.
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The association of Src, EGFR and beta1 integrin is dependent upon membrane traffic that is mediated by syntaxin13 (officially known as STX12) and SNAP23.
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Data suggest SNAP23 and VAMP3 (vesicle-associated membrane protein 3) participate in interleukin-1beta-, interleukin-1 receptor-, calcium signaling-dependent secretion/exocytosis of interleukin-6 and tumor necrosis factor alpha from synoviocytes.
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Results suggest that phagosomal SNAP-23 is one of the key players regulating the phagosomal environment in macrophages.
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STX-3 and SNAP-23 are crucial for the release of all chemokines in mature human mast cells
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Data show that knockdown of SNAP-23 inhibited the production of virus.
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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.
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SNAP23 and SNAP25 palmitoylation is regulated by DHHC palmitoyl transferases
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the importance of SNAP23 in the trafficking of matrix metalloproteinases during degradation of extracellular matrix substrates and subsequent cellular invasion