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Syntaxin-2, also known as epimorphin, is a protein that in humans is encoded by the STX2 gene.[1][2][3]

The product of this gene belongs to the syntaxin/epimorphin family of proteins. The syntaxins are a large protein family implicated in the targeting and fusion of intracellular transport vesicles. The product of this gene regulates epithelial-mesenchymal interactions and epithelial cell morphogenesis and activation. Alternatively spliced transcript variants encoding different isoforms have been identified.[3] When the N terminus is on the cytosolic face it acts as a t-SNARE involved in intracellular vesicle docking and is called Syntaxin-2. When flipped inside out, i.e. N terminus hangs out on the extracellular surface (by some nonclassical secretion pathway) it acts as a versatile morphogen and is called epimorphin. This membrane protein enjoys the double choice of another form of topological alternatives of being targeted to either apical or basolateral surface of an epithelial cell in a regulated way depending on various contexts. When expressed by mesenchymal cells it can instruct epithelial morphogenesis at epithelial mesenchymal interfaces.


STX2 has been shown to interact with SNAP-25,[4][5] SNAP23,[5][6][7][8] STXBP1[4][9] and Syntaxin binding protein 3.[9]


  1. Zha H, Remmers EF, Szpirer C, Szpirer J, Zhang H, Kozak CA, Wilder RL (Nov 1996). "The epimorphin gene is highly conserved among humans, mice, and rats and maps to human chromosome 7, mouse chromosome 5, and rat chromosome 12". Genomics. 37 (3): 386–9. doi:10.1006/geno.1996.0574. PMID 8938452.
  2. Band AM, Kuismanen E (Jun 2005). "Localization of plasma membrane t-SNAREs syntaxin 2 and 3 in intracellular compartments". BMC Cell Biology. 6 (1): 26. doi:10.1186/1471-2121-6-26. PMC 1156879. PMID 15943887.
  3. 3.0 3.1 "Entrez Gene: STX2 syntaxin 2".
  4. 4.0 4.1 Hata Y, Südhof TC (Jun 1995). "A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic". The Journal of Biological Chemistry. 270 (22): 13022–8. doi:10.1074/jbc.270.22.13022. PMID 7768895.
  5. 5.0 5.1 Ravichandran V, Chawla A, Roche PA (Jun 1996). "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". The Journal of Biological Chemistry. 271 (23): 13300–3. doi:10.1074/jbc.271.23.13300. PMID 8663154.
  6. Imai A, Nashida T, Yoshie S, Shimomura H (Aug 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Archives of Oral Biology. 48 (8): 597–604. doi:10.1016/S0003-9969(03)00116-X. PMID 12828989.
  7. Li G, Alexander EA, Schwartz JH (May 2003). "Syntaxin isoform specificity in the regulation of renal H+-ATPase exocytosis". The Journal of Biological Chemistry. 278 (22): 19791–7. doi:10.1074/jbc.M212250200. PMID 12651853.
  8. Araki S, Tamori Y, Kawanishi M, Shinoda H, Masugi J, Mori H, Niki T, Okazawa H, Kubota T, Kasuga M (May 1997). "Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c". Biochemical and Biophysical Research Communications. 234 (1): 257–62. doi:10.1006/bbrc.1997.6560. PMID 9168999.
  9. 9.0 9.1 Schraw TD, Lemons PP, Dean WL, Whiteheart SW (Aug 2003). "A role for Sec1/Munc18 proteins in platelet exocytosis". The Biochemical Journal. 374 (Pt 1): 207–17. doi:10.1042/BJ20030610. PMC 1223584. PMID 12773094.

Further reading