The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

STX4  -  syntaxin 4

Homo sapiens

Synonyms: Renal carcinoma antigen NY-REN-31, STX4A, Syntaxin-4, p35-2
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of STX4

  • Within the syntaxin family, syntaxin 4 interacted with SNAP23 and all vesicle-associated membrane proteins (VAMPs) examined, except tetanus neurotoxin insensitive VAMP (TI-VAMP) [1].
 

High impact information on STX4

  • The vesicle-targeting proteins synaptobrevin-2 and syntaxin-4 are proposed to play roles in this process [2].
  • Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes [3].
  • In contrast, the carboxyterminal domain of Synip does not dissociate from syntaxin 4 in response to insulin stimulation but inhibits glucose transport and GLUT4 translocation [3].
  • Addition of PA to Stx4/SNAP23 vesicles markedly enhanced the fusion rate, whereas its addition to VAMP2 vesicles was inhibitory [4].
  • When syntaxin-4 is modeled into the synaptic fusion complex as a replacement of syntaxin-1A, no major steric clashes arise and the most variable amino acids localize to the outer surface of the complex [5].
 

Biological context of STX4

  • These data indicate that VAMP-2 mediates exocytosis of specific and tertiary granules, and that Q-SNARE/R-SNARE complexes containing VAMP-2 and syntaxin 4 are involved in neutrophil exocytosis [6].
  • These data demonstrate that syntaxin 4 plays a functional role on insulin release and granule fusion in beta cells and that this process is regulated by the syntaxin 4-specific binding protein Synip [7].
  • The PKC-dependent phosphorylation of PSP in activated platelets and its inhibitory effects on syntaxin 4 binding provide a novel functional link that may be important in coupling the processes of cell activation, intracellular signaling, and secretion [8].
  • We observed that during phagocytosis, Rab5a in GTP-bound form interacted with syntaxin-4 on the membrane of MCP and were retained for up to 90 minutes, whereas the complex was recruited to the SCP within 5 minutes but was selectively depleted from these vacuoles after 30 minutes of phagocytosis [9].
  • RESULTS: Nucleotide sequences obtained from PCR products exhibited nearly identical (>95%) homology with reported sequences for human SNAP-23 and syntaxin-4 [10].
 

Anatomical context of STX4

 

Associations of STX4 with chemical compounds

  • Consistent with a functional role of syntaxin 4 in this process, expression of syntaxin 4/DeltaTM also inhibited glucose-stimulated insulin secretion [7].
  • In contrast, addition of PIP2 to Stx4/SNAP23 vesicles inhibited the fusion reaction, and its addition to VAMP2 vesicles was stimulatory [4].
  • Cholesterol depletion causes dispersion of syntaxin 3 but not syntaxin 4 clusters [14].
  • We found that syntaxin 4 was phosphorylated in human platelets treated with a physiologic agent that induces secretion (thrombin) but not when they were treated with an agent that prevents secretion (prostacyclin) [15].
  • In contrast, calpeptin did not prevent SFLLRN-induced degradation of VAMP-3 and syntaxin 4 did not undergo substantial proteolysis following platelet activation [16].
 

Physical interactions of STX4

 

Co-localisations of STX4

 

Regulatory relationships of STX4

 

Other interactions of STX4

 

Analytical, diagnostic and therapeutic context of STX4

References

  1. Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment. Paumet, F., Le Mao, J., Martin, S., Galli, T., David, B., Blank, U., Roa, M. J. Immunol. (2000) [Pubmed]
  2. Regulation of aquaporin-2 water channel trafficking by vasopressin. Knepper, M.A., Inoue, T. Curr. Opin. Cell Biol. (1997) [Pubmed]
  3. Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes. Min, J., Okada, S., Kanzaki, M., Elmendorf, J.S., Coker, K.J., Ceresa, B.P., Syu, L.J., Noda, Y., Saltiel, A.R., Pessin, J.E. Mol. Cell (1999) [Pubmed]
  4. Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion. Vicogne, J., Vollenweider, D., Smith, J.R., Huang, P., Frohman, M.A., Pessin, J.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Fasshauer, D., Sutton, R.B., Brunger, A.T., Jahn, R. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  6. Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils. Mollinedo, F., Martín-Martín, B., Calafat, J., Nabokina, S.M., Lazo, P.A. J. Immunol. (2003) [Pubmed]
  7. Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate insulin secretion in the pancreatic beta HC-9 cell. Saito, T., Okada, S., Yamada, E., Ohshima, K., Shimizu, H., Shimomura, K., Sato, M., Pessin, J.E., Mori, M. J. Biol. Chem. (2003) [Pubmed]
  8. Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion. Reed, G.L., Houng, A.K., Fitzgerald, M.L. Blood (1999) [Pubmed]
  9. Rab5a GTPase regulates fusion between pathogen-containing phagosomes and cytoplasmic organelles in human neutrophils. Perskvist, N., Roberg, K., Kulyté, A., Stendahl, O. J. Cell. Sci. (2002) [Pubmed]
  10. Expression of eosinophil target SNAREs as potential cognate receptors for vesicle-associated membrane protein-2 in exocytosis. Logan, M.R., Lacy, P., Bablitz, B., Moqbel, R. J. Allergy Clin. Immunol. (2002) [Pubmed]
  11. Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments. Brumell, J.H., Volchuk, A., Sengelov, H., Borregaard, N., Cieutat, A.M., Bainton, D.F., Grinstein, S., Klip, A. J. Immunol. (1995) [Pubmed]
  12. Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2. Jagadish, M.N., Fernandez, C.S., Hewish, D.R., Macaulay, S.L., Gough, K.H., Grusovin, J., Verkuylen, A., Cosgrove, L., Alafaci, A., Frenkel, M.J., Ward, C.W. Biochem. J. (1996) [Pubmed]
  13. A critical role for vesicle-associated membrane protein-7 in exocytosis from human eosinophils and neutrophils. Logan, M.R., Lacy, P., Odemuyiwa, S.O., Steward, M., Davoine, F., Kita, H., Moqbel, R. Allergy (2006) [Pubmed]
  14. Syntaxins 3 and 4 are concentrated in separate clusters on the plasma membrane before the establishment of cell polarity. Low, S.H., Vasanji, A., Nanduri, J., He, M., Sharma, N., Koo, M., Drazba, J., Weimbs, T. Mol. Biol. Cell (2006) [Pubmed]
  15. Protein kinase C phosphorylation of syntaxin 4 in thrombin-activated human platelets. Chung, S.H., Polgar, J., Reed, G.L. J. Biol. Chem. (2000) [Pubmed]
  16. SNARE protein degradation upon platelet activation: calpain cleaves SNAP-23. Lai, K.C., Flaumenhaft, R. J. Cell. Physiol. (2003) [Pubmed]
  17. Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion. Polgár, J., Chung, S.H., Reed, G.L. Blood (2002) [Pubmed]
  18. Involvement of syntaxin 4 in the transport of membrane-type 1 matrix metalloproteinase to the plasma membrane in human gastric epithelial cells. Miyata, T., Ohnishi, H., Suzuki, J., Yoshikumi, Y., Ohno, H., Mashima, H., Yasuda, H., Ishijima, T., Osawa, H., Satoh, K., Sunada, K., Kita, H., Yamamoto, H., Sugano, K. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  19. Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton. Band, A.M., Ali, H., Vartiainen, M.K., Welti, S., Lappalainen, P., Olkkonen, V.M., Kuismanen, E. FEBS Lett. (2002) [Pubmed]
  20. Phosphorylation of SNAP-23 in activated human platelets. Polgár, J., Lane, W.S., Chung, S.H., Houng, A.K., Reed, G.L. J. Biol. Chem. (2003) [Pubmed]
  21. Interaction of the taxilin family with the nascent polypeptide-associated complex that is involved in the transcriptional and translational processes. Yoshida, K., Nogami, S., Satoh, S., Tanaka-Nakadate, S., Hiraishi, H., Terano, A., Shirataki, H. Genes Cells (2005) [Pubmed]
  22. Combinatorial SNARE complexes modulate the secretion of cytoplasmic granules in human neutrophils. Mollinedo, F., Calafat, J., Janssen, H., Martín-Martín, B., Canchado, J., Nabokina, S.M., Gajate, C. J. Immunol. (2006) [Pubmed]
  23. Pancreatic Acinar Cells Express Vesicle-associated Membrane Protein 2- and 8-Specific Populations of Zymogen Granules with Distinct and Overlapping Roles in Secretion. Weng, N., Thomas, D.D., Groblewski, G.E. J. Biol. Chem. (2007) [Pubmed]
  24. Protease-activated receptor-1 activation of endothelial cells induces protein kinase Calpha-dependent phosphorylation of syntaxin 4 and Munc18c: role in signaling p-selectin expression. Fu, J., Naren, A.P., Gao, X., Ahmmed, G.U., Malik, A.B. J. Biol. Chem. (2005) [Pubmed]
  25. Identification and cloning of the SNARE proteins VAMP-2 and syntaxin-4 from HL-60 cells and human neutrophils. Smolen, J.E., Hessler, R.J., Nauseef, W.M., Goedken, M., Joe, Y. Inflammation (2001) [Pubmed]
  26. Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. Tellam, J.T., Macaulay, S.L., McIntosh, S., Hewish, D.R., Ward, C.W., James, D.E. J. Biol. Chem. (1997) [Pubmed]
 
WikiGenes - Universities