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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. Zusätzlich bieten wir Ihnen Synaptosomal-Associated Protein, 23kDa Antikörper (133) und und viele weitere Produktgruppen zu diesem Protein an.
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PKM2 (zeige PKM Proteine) promotes tumor cell exosome release via phosphorylating protein SNAP23.
These results demonstrate opposing roles for SNAP23 in the secretion mechanisms of the endocrine and exocrine pancreas.
SNAP23 is selectively expressed in airway secretory cells and mediates baseline and stimulated mucin (zeige SLC13A2 Proteine) secretion.
these data suggest that SNAP23 is a key component of the endothelial SNARE (zeige VTI1B Proteine) machinery that mediates endothelial exocytosis.
Data indicate that acute depletion of synaptosomal-associated protein 23 (SNAP-23) in fibroblasts leads to rapid apoptotic cell death.
Use of neurons from double-knock-out (SNAP-25 (zeige SNAP25 Proteine), synaptotagmin-7 (zeige SYT7 Proteine)) mice in combination with viral transduction showed that SNAP-23-driven release is triggered by endogenous synaptotagmin-7 (zeige SYT7 Proteine)
Results suggest that Plin2 (zeige PLIN2 Proteine) inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets.
morphine suppresses TLR4 (zeige TLR4 Proteine)-induced TNF (zeige TNF Proteine) release in mast cells, preventing the IKK (zeige CHUK Proteine)-dependent phosphorylation of SNAP-23, which is necessary for TNF (zeige TNF Proteine) exocytosis, and this inhibition correlates with the formation of a beta (zeige SUCLA2 Proteine)-arrestin-2 (zeige ARRB2 Proteine)/TRAF6 (zeige TRAF6 Proteine) complex
We report the regulation of platelet secretion via phosphorylation of SNAP-23 at Ser95.
Results suggest that phagosomal SNAP-23 is one of the key players regulating the phagosomal environment in macrophages.
SNAP23 suppressed progression of cervical cancer and induced cell cycle G2/M arrest via upregulating p21(cip1 (zeige CDKN1A Proteine)) and downregulating CyclinB1
Knockdown of VAMP3 (zeige VAMP3 Proteine) and SNAP23 reduces endothelial secretion of miR (zeige MLXIP Proteine)-126-3p and miR (zeige MLXIP Proteine)-200a-3p, as well as the proliferation, migration, and suppression of contractile markers in smooth muscle cells caused by vascular endothelial cell-coculture.
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.
A novel regulatory mechanism for SNAP23-dependent mast cell activation of T. vaginalis-secreted LTB4 involving surface trafficking of BLT1.
Study identified SNAP23 as a novel oncogene (zeige RAB1A Proteine) in Ovarian Cancer (OC). It is over-expressed in OC and could promote the proliferation, migration and invasion of OC in vitro.
Localization of SNAP23 was found in plasma membrane, lipid droplets and mitochondria of skeletal muscle.
these data suggest that SNAP23 is a key component of the endothelial SNARE (zeige NAPA Proteine) machinery that mediates endothelial exocytosis.
Increased level of SNAP23-Syntaxin4 (zeige STX4 Proteine)-VAMP7 (zeige VAMP7 Proteine) interaction correlates with decreased Syntaxin4 (zeige STX4 Proteine) phosphorylation and trafficking of MT1-MMP (zeige MMP14 Proteine) to invadopodia during cellular invasion.
The association of Src (zeige SRC Proteine), EGFR (zeige EGFR Proteine) and beta1 integrin is dependent upon membrane traffic that is mediated by syntaxin13 (officially known as STX12 (zeige STX12 Proteine)) and SNAP23.
mRNA levels of BSCL2 (zeige BSCL2 Proteine) and SNAP23, but not COPA (zeige COPA Proteine), increased during adipocyte differentiation. Redistribution of SNAP23 protein to different cellular compartments was observed when comparing undifferentiated mesenchymal stem cells and differentiated adipocytes.
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.
synaptosomal-associated protein 23
, synaptosomal-associated protein 23 isoform SNAP23A
, synaptosomal-associated protein, 23kDa
, synaptosomal-associated protein, 23kD
, vesicle-membrane fusion protein SNAP-23
, synaptosomal-associated protein 23 kD
, synaptosomal-associated protein, 23 kD