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Gene Review

Stx4  -  syntaxin 4

Rattus norvegicus

Synonyms: Stx4a, Syntaxin-4
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High impact information on Stx4a

  • Together, our data suggest that insulin induces remodeling of the fodrin-actin network, which is required for the fusion of GLUT4 storage vesicles with the plasma membrane by permitting their access to the t-SNARE syntaxin 4 [1].
  • We show that fodrin interacts with the t-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) syntaxin 4, and this interaction is increased by insulin stimulation and decreased by prior latrunculin A treatment [1].
  • Here we show that Ca2+-dependent interaction of the synaptotagmin VII C(2)A domain with SNAP-23 is facilitated by syntaxin 4 [2].
  • Lysosomal exocytosis was inhibited by the SNARE domains of syntaxin 4 and TI-VAMP/VAMP7 and by cleavage of SNAP-23 with botulinum neurotoxin E, thereby functionally implicating these SNAREs in Ca2+-regulated exocytosis of conventional lysosomes [2].
  • Increased cellular levels of the soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins syntaxin 4 and vesicle-associated membrane protein (VAMP)-2 were also observed in the insulin-resistant SHRSP strain [3].

Biological context of Stx4a


Anatomical context of Stx4a

  • Syntaxin 4 mRNA is expressed in selective tissues including rat skeletal muscle, although it has not been studied at the protein level in any cell type [7].
  • The content of the syntaxin 4 protein increased by 1.9-fold during differentiation of L6 myoblasts into myotubes [7].
  • Therefore, we generated an affinity-purified antibody against syntaxin 4 to demonstrate that this 36 kDa protein is expressed in rat skeletal muscle and L6 muscle cells in culture [7].
  • While syntaxin 4 localizes all along the basal and lateral plasma membrane domains in vivo, it is restricted to the lateral membrane in Madin-Darby canine kidney (MDCK) cells in two-dimensional monolayer culture [8].
  • When cultured as cysts in collagen, however, MDCK cells target syntaxin 4 correctly to the basal and lateral membranes [8].

Associations of Stx4a with chemical compounds

  • Restoration of normoglycemia and normoinsulinemia in ZDF rats with rosiglitazone (30 micromol/kg) normalized cellubrevin, VAMP-2, and syntaxin 4 protein to levels approaching those observed in lean control animals [5].

Physical interactions of Stx4a

  • In addition, a stretch of 12 amino acids in the middle of the SNARE motif of syntaxin 1A was able to confer binding activity to the non-binding relative syntaxin 4 [9].
  • Associated kinase activity, which diminishes after stimulation as a consequence of intracellular calcium increases, specifically phosphorylates syntaxin 4 thereby affecting its capacity to bind to its t-SNARE partner SNAP-23 [6].

Other interactions of Stx4a


Analytical, diagnostic and therapeutic context of Stx4a


  1. Role of Insulin-dependent Cortical Fodrin/Spectrin Remodeling in Glucose Transporter 4 Translocation in Rat Adipocytes. Liu, L., Jedrychowski, M.P., Gygi, S.P., Pilch, P.F. Mol. Biol. Cell (2006) [Pubmed]
  2. Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis. Rao, S.K., Huynh, C., Proux-Gillardeaux, V., Galli, T., Andrews, N.W. J. Biol. Chem. (2004) [Pubmed]
  3. Skeletal muscle of stroke-prone spontaneously hypertensive rats exhibits reduced insulin-stimulated glucose transport and elevated levels of caveolin and flotillin. James, D.J., Cairns, F., Salt, I.P., Murphy, G.J., Dominiczak, A.F., Connell, J.M., Gould, G.W. Diabetes (2001) [Pubmed]
  4. Retinal pigment epithelial cells exhibit unique expression and localization of plasma membrane syntaxins which may contribute to their trafficking phenotype. Low, S.H., Marmorstein, L.Y., Miura, M., Li, X., Kudo, N., Marmorstein, A.D., Weimbs, T. J. Cell. Sci. (2002) [Pubmed]
  5. v- and t-SNARE protein expression in models of insulin resistance: normalization of glycemia by rosiglitazone treatment corrects overexpression of cellubrevin, vesicle-associated membrane protein-2, and syntaxin 4 in skeletal muscle of Zucker diabetic fatty rats. Maier, V.H., Melvin, D.R., Lister, C.A., Chapman, H., Gould, G.W., Murphy, G.J. Diabetes (2000) [Pubmed]
  6. SNAREs and associated regulators in the control of exocytosis in the RBL-2H3 mast cell line. Blank, U., Cyprien, B., Martin-Verdeaux, S., Paumet, F., Pombo, I., Rivera, J., Roa, M., Varin-Blank, N. Mol. Immunol. (2002) [Pubmed]
  7. Expression of syntaxin 4 in rat skeletal muscle and rat skeletal muscle cells in culture. Sumitani, S., Ramlal, T., Liu, Z., Klip, A. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  8. SNARE expression and localization in renal epithelial cells suggest mechanism for variability of trafficking phenotypes. Li, X., Low, S.H., Miura, M., Weimbs, T. Am. J. Physiol. Renal Physiol. (2002) [Pubmed]
  9. Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. Pabst, S., Hazzard, J.W., Antonin, W., Südhof, T.C., Jahn, R., Rizo, J., Fasshauer, D. J. Biol. Chem. (2000) [Pubmed]
  10. SNARE complex proteins, including the cognate pair VAMP-2 and syntaxin-4, are expressed in cultured oligodendrocytes. Madison, D.L., Krueger, W.H., Cheng, D., Trapp, B.D., Pfeiffer, S.E. J. Neurochem. (1999) [Pubmed]
  11. Interaction of SNARE proteins in rat parotid acinar cells. Takuma, T., Arakawa, T., Tajima, Y. Arch. Oral Biol. (2000) [Pubmed]
  12. Identification of the molecular mechanisms contributing to polarized trafficking in osteoblasts. Prêle, C.M., Horton, M.A., Caterina, P., Stenbeck, G. Exp. Cell Res. (2003) [Pubmed]
  13. Expression of syntaxins in rat kidney. Mandon, B., Nielsen, S., Kishore, B.K., Knepper, M.A. Am. J. Physiol. (1997) [Pubmed]
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