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Syntaxin 4

syntaxin 4, syn-4
involved in docking of synaptic vesicles at presynaptic active zones [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: SNAP-23, Insulin, VAMP2, SNAP-25, V1a
Papers using syntaxin 4 antibodies
Insulin-like growth factor-I inhibits transcriptional responses of transforming growth factor-beta by phosphatidylinositol 3-kinase/Akt-dependent suppression of the activation of Smad3 but not Smad2.
Nurminsky Dmitry I., In PLoS ONE, 2002
... 03, 1005), Glucose-6-P dehydrogenase (Abcam, ab34436), Protein Kinase C-zeta (Cell signaling, ab51157), P-PKC-zeta (Abcam, ab76129), Syntaxin 4 (Abcam, ab57841), Vamp2 (Abcam, ab3347), ...
Hydrogen peroxide regulation of endothelial exocytosis by inhibition of N-ethylmaleimide sensitive factor
Lowenstein Charles J. et al., In The Journal of Cell Biology, 1999
... Mouse mAbs to NSF and syntaxin-4 were purchased from BD Biosciences.
Papers on syntaxin 4
Characterization of α-taxilin as a novel factor controlling the release of hepatitis C virus.
Hildt et al., Langen, Germany. In Biochem J, Feb 2016
α-Taxilin was identified as a novel binding partner of syntaxin-4 and of other members of the syntaxin family, which are part of SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) complexes and so are involved in intracellular vesicle traffic.
Tctex1d2 Is a Negative Regulator of GLUT4 Translocation and Glucose Uptake.
Yamada et al., Japan. In Endocrinology, Oct 2015
Although overexpression of Tctex1d2 had no significant effect on GLUT4 internalization, Tctex1d2 was found to associate with syntaxin 4 in an insulin-dependent manner and inhibit Doc2b binding to syntaxin 4. In addition, glucose-dependent insulinotropic polypeptide rescued the Tctex1d2 inhibition of insulin-stimulated GLUT4 translocation by suppressing the Tctex1d2-syntaxin 4 interaction and increasing Doc2b-Synatxin4 interactions.
Tomosyn is a novel Akt substrate mediating insulin-dependent GLUT4 exocytosis.
Hirata et al., Fukuoka, Japan. In Int J Biochem Cell Biol, May 2015
In vitro pull-down assay showed that phosphorylation of tomosyn at Ser-783 by Akt inhibited the interaction with syntaxin 4. Insulin stimulation increased GLUT4 in the cell surface of CHO-K1 cells to promote glucose uptake, however exogenous expression of the mutant tomosyn attenuated the increase by insulin.
Effect of Resveratrol Supplementation on the SNARE Proteins Expression in Adipose Tissue of Stroptozotocin-Nicotinamide Induced Type 2 Diabetic Rats.
Shabab et al., Hamadān, Iran. In Iran J Med Sci, May 2015
Isoforms of the SNAP23, syntaxin-4 and VAMP-2 play an important role in regulating GLUT-4 trafficking and fusion in adipocytes.
Munc18c mediates exocytosis of pre-docked and newcomer insulin granules underlying biphasic glucose stimulated insulin secretion in human pancreatic beta-cells.
Gaisano et al., Toronto, Canada. In Mol Metab, May 2015
Munc18c-KD caused reduction in cognate syntaxin-4 islet expression but not in other exocytotic proteins, resulting in the reduction in GSIS in first- (by 42%) and second phases (by 35%).
Retinoic Acid and LTP Recruit Postsynaptic AMPA Receptors Using Distinct SNARE-Dependent Mechanisms.
Chen et al., Stanford, United States. In Neuron, May 2015
Specifically, RA-induced AMPAR trafficking did not involve complexin, which activates SNARE complexes containing syntaxin-1 or -3, but not complexes containing syntaxin-4, whereas LTP required complexin.
Blocking the expression of syntaxin 4 interferes with initial phagocytosis of Brucella melitensis in macrophages.
Verdugo-Rodríguez et al., Texcoco de Mora, Mexico. In Can J Vet Res, 2015
Abstract available from the publisher.
Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE Complexes.
Kumar et al., Hattiesburg, United States. In Plos One, 2014
Here we undertake a comprehensive examination of the capacity of two Q-SNARE subcomplexes (syntaxin3/SNAP-23 and syntaxin4/SNAP-23) to form fusogenic trans-SNARE complexes with each of the four granule-borne R-SNAREs (VAMP2, 3, 7, 8).
Regulation of mucosal mast cell activation by short interfering RNAs targeting syntaxin4.
Maeyama et al., Japan. In Immunol Cell Biol, 2012
regulation of mucosal mast cell activation
The impact of extracellular syntaxin4 on HaCaT keratinocyte behavior.
Hirai et al., Japan. In Biochem Biophys Res Commun, 2012
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 and syntaxin4 on keratinocyte cornification.
Gelsolin associates with the N terminus of syntaxin 4 to regulate insulin granule exocytosis.
Thurmond et al., Indianapolis, United States. In Mol Endocrinol, 2012
data support a mechanistic model for gelsolin's role in insulin exocytosis: gelsolin clamps unsolicited soluble N-ethylmaleimide-sensitive factor attachment receptor-regulated exocytosis through association with Syn4 which is relieved upon stimulus-induced calcium influx to activate gelsolin to facilitate insulin exocytosis
Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells.
Savina et al., Paris, France. In Cell, 2012
Sec22b localizes to the ER-Golgi intermediate compartment (ERGIC) and pairs to the plasma membrane SNARE syntaxin 4, which is present in phagosomes (Phgs).
Syntaxins 3 and 4 mediate vesicular trafficking of α5β1 and α3β1 integrins and cancer cell migration.
Hu et al., Louisville, United States. In Int J Oncol, 2011
siRNA knockdown (KD) of syntaxins 3 and 4 in HeLa cells reduced cell surface expression of alpha5beta1 and alpha3beta1 integrins
Stimulus-induced S-nitrosylation of Syntaxin 4 impacts insulin granule exocytosis.
Thurmond et al., Indianapolis, United States. In J Biol Chem, 2011
Syntaxin 4 activation and insulin release in the absence of the glucose stimulus, consistent with nitrosative stress and dysfunctional exocytosis
Syntaxin-4 defines a domain for activity-dependent exocytosis in dendritic spines.
Ehlers et al., Durham, United States. In Cell, 2010
Stx4 defines an exocytic zone that directs membrane fusion for postsynaptic plasticity, revealing a novel specialization for local membrane traffic in dendritic spines.
Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4.
Thurmond et al., Indianapolis, United States. In Am J Physiol Regul Integr Comp Physiol, 2010
The process of insulin secretion uses multiple Munc18-syntaxin isoform pairs, whereas insulin action in the peripheral tissues appears to use only the Munc18c-syntaxin 4 pair.
Role of syntaxin 4 in activity-dependent exocytosis and synaptic plasticity in hippocampal neurons.
Shanmugam et al., Tiruchchirāppalli, India. In Sci Signal, 2009
Stx4 is an essential postsynaptic component for synaptic plasticity in hippocampal neurons.
Glucose transporter 4: cycling, compartments and controversies.
Klip et al., Toronto, Canada. In Embo Rep, 2005
In particular, fusion seems to be regulated by aPKC (via munc18) and Akt (via syntaxin4-interacting protein (synip)).
Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners.
Klip et al., Toronto, Canada. In Endocrinology, 2005
At the cell periphery, GLUT4-containing vesicles tether, dock, and fuse with the PM assisted by the exocyst complex followed by engagement of a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex [with vesicle-associated membrane protein (VAMP)2 as the vesicular (v)-SNARE and soluble NSF-attachment protein (SNAP)23 and syntaxin4 as target (t)-SNAREs] regulated by the accessory proteins Munc18c, Synip and Tomosyn.
The epithelium in inflammatory bowel disease: potential role of endocytosis of junctional proteins in barrier disruption.
Parkos et al., Atlanta, United States. In Novartis Found Symp, 2003
Interestingly, internalized AJ and TJ proteins enter early endosomes followed by movement to organelles that do not label with markers of late and recycling endosomes, lysosomes or Golgi but appear to represent a unique storage compartment that colocalizes with t-SNARE protein, syntaxin 4. A better understanding of the mechanisms of junctional internalization and recycling will likely provide new insights into the mechanisms of altered barrier function in IBD.
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