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Data suggest MUNC18C (show STXBP3 Proteins) is required for STX4-mediated invadopodium formation and tumor invasion of extracellular matrix; N-terminal STX4 fragment binds to MUNC18C (show STXBP3 Proteins) and inhibits interactions of STX4 with synaptosome-associated protein 23 (SNAP23 (show SNAP23 Proteins)) and vesicle-associated membrane protein 2 (VAMP2 (show VAMP2 Proteins)). Fibrosarcoma/adenocarcinoma cell lines were used in these studies. (MUNC18C (show STXBP3 Proteins) = syntaxin binding protein MUNC18C (show STXBP3 Proteins); STX4 = syntaxin 4)
The analysis revealed three candidate genes GSK3B, PTPN1 (show PTPN1 Proteins), STX4 that are differentially expressed in study subjects. GSK3B was highly significant in Ps-T2D (P=0.00018, FR=-26.6), followed by Ps (P=0.0028, FR=-14.5) and T2D groups (P=0.032, FR=-5.9). PTPN1 (show PTPN1 Proteins) showed significant association only with PS-T2D (P=0.00027, FR=-8.5). STX4 showed significant association with both Ps (P=0.0002, FR=-20) and Ps-T2D (P=0.0016, FR=-11.2).
When the expression of STX4 mRNA was inhibited with short or small interfering, or silencing, RNA in macrophages, the survival of Brucella melitensis was significantly reduced.
Syntaxin-4 has a role in mediating exocytosis of pre-docked and newcomer insulin (show INS Proteins) granules underlying biphasic glucose-stimulated insulin (show INS Proteins) secretion in human pancreatic beta cells
Increased level of SNAP23 (show SNAP23 Proteins)-Syntaxin4-VAMP7 (show VAMP7 Proteins) interaction correlates with decreased Syntaxin4 phosphorylation and trafficking of MT1-MMP (show MMP14 Proteins) to invadopodia during cellular invasion.
upregulation of Syntaxin 4 is sufficient to significantly improve insulin (show INS Proteins) secretory function to human type 2 diabetes islets retaining low levels of residual function
STX4 is implicated in the antibody secretion.
Syntaxin-4 plays a vital role in exocytosis of IgE from plasma cells. Knock-down of syntaxin-4, but not VAMP3 dramatically reduced IgE secretion from U266 plasma cells causing it to accumulate in the cell.
These results revealed, for the first time, the extracellular role of syntaxin4 and shed light on the division of the extracellular effects exerted by epimorphin (show STX2 Proteins) and syntaxin4 on keratinocyte cornification.
Syntaxin 4 activation and insulin (show INS Proteins) release in the absence of the glucose stimulus, consistent with nitrosative stress and dysfunctional exocytosis
Syntaxin-4 not only bound to laminin but also latched onto the glycosaminoglycan side chains of syndecan-1 (show SDC1 Proteins), a laminin receptor that mediates epithelial morphogenesis. Thus, temporal extracellular extrusion of syntaxin-4 emerged as a novel regulatory element for laminin-induced mammary epithelial cell behaviors.
Syn4 transgenic mice with high level expression of Syn4 had a significant extension of lifespan (33% increase in median) and showed increased peripheral insulin (show INS Proteins) sensitivity, even at ages where controls exhibited age-related insulin (show INS Proteins) resistance.
Non-directional stimulation with extracellular syntaxin-4 induces a dramatic morphological change in teratocarcinoma F9 cells and in several endodermal markers, both of which effects are reminiscent of the cells treated with all-trans retinoic acid.
Delivery of GLUT4 (show SLC2A4 Proteins) to the plasma membrane is mediated by formation of functional SNARE (show VTI1B Proteins) complexes containing syntaxin4, SNAP23 (show SNAP23 Proteins), and VAMP2 (show VAMP2 Proteins).
data support a mechanistic model for gelsolin's role in insulin (show INS Proteins) exocytosis: gelsolin (show GSN Proteins) clamps unsolicited soluble N-ethylmaleimide-sensitive factor (show NSF Proteins) attachment receptor-regulated exocytosis through association with Syn4 which is relieved upon stimulus-induced calcium influx to activate gelsolin (show GSN Proteins) to facilitate insulin (show INS Proteins) exocytosis
functions as the necessary t-SNARE (show VTI1B Proteins) protein responsible for correct fusion of the GLUT8 (show SLC2A8 Proteins)-containing vesicle with the plasma membrane in the mouse blastocyst
Interacts with tomosyn (show STXBP5 Proteins) and plays a role in insulin (show INS Proteins)-stimulated GLUT4 (show SLC2A4 Proteins) translocation.
female Syn4 transgenic mice exhibited an increased rate of glucose clearance during glucose tolerance tests that was repressible by the administration of tetracycline
Data show that Munc18c (show STXBP3 Proteins) binds to monomeric syntaxin4 and the N-terminal 29 amino acids of syntaxin4 are necessary for this interaction.
Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity).
, syntaxin 4
, renal carcinoma antigen NY-REN-31
, syntaxin 4A (placental)