Biology:SNAP23

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene.[1][2] Two alternative transcript variants encoding different protein isoforms have been described for this gene.

Function

Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues.

SNAP23 is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion.[3]

Clinical significance

In individuals with insulin resistance, SNAP23 is found to be translocated from the plasma membrane to the cytosol where it becomes associated with lipid droplets and is therefore unable to translocate GLUT-4 to the membrane, hindering glucose transport.

Interactions

SNAP23 has been shown to interact with:

References

  1. ↑ "Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells". Biochemical and Biophysical Research Communications 231 (3): 808–12. Feb 1997. doi:10.1006/bbrc.1997.6196. PMID 9070898. Bibcode: 1997BBRC..231..808M. 
  2. ↑ 2.0 2.1 2.2 2.3 2.4 "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. Jun 1996. doi:10.1074/jbc.271.23.13300. PMID 8663154. 
  3. ↑ "Entrez Gene: SNAP23 synaptosomal-associated protein, 23kDa". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8773. 
  4. ↑ "CFTR chloride channels are regulated by a SNAP-23/syntaxin 1A complex". Proceedings of the National Academy of Sciences of the United States of America 99 (19): 12477–82. Sep 2002. doi:10.1073/pnas.192203899. PMID 12209004. Bibcode: 2002PNAS...9912477C. 
  5. ↑ "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry 41 (50): 14906–15. Dec 2002. doi:10.1021/bi026417u. PMID 12475239. 
  6. ↑ 6.0 6.1 "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R. 
  7. ↑ "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells". The Biochemical Journal 375 (Pt 2): 433–40. Oct 2003. doi:10.1042/BJ20030427. PMID 12877659. 
  8. ↑ "Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network". Journal of Cell Science 112 (6): 845–54. Mar 1999. doi:10.1242/jcs.112.6.845. PMID 10036234. 
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 9.6 "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. Aug 2003. doi:10.1016/S0003-9969(03)00116-X. PMID 12828989. 
  10. ↑ 10.0 10.1 10.2 "Syntaxin isoform specificity in the regulation of renal H+-ATPase exocytosis". The Journal of Biological Chemistry 278 (22): 19791–7. May 2003. doi:10.1074/jbc.M212250200. PMID 12651853. 
  11. ↑ 11.0 11.1 11.2 11.3 "Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c". Biochemical and Biophysical Research Communications 234 (1): 257–62. May 1997. doi:10.1006/bbrc.1997.6560. PMID 9168999. Bibcode: 1997BBRC..234..257A. 
  12. ↑ 12.0 12.1 12.2 "Three novel proteins of the syntaxin/SNAP-25 family". The Journal of Biological Chemistry 273 (51): 34171–9. Dec 1998. doi:10.1074/jbc.273.51.34171. PMID 9852078. 
  13. ↑ 13.0 13.1 13.2 13.3 "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". Journal of Immunology 164 (11): 5850–7. Jun 2000. doi:10.4049/jimmunol.164.11.5850. PMID 10820264. 
  14. ↑ 14.0 14.1 "Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2". The Journal of Biological Chemistry 275 (11): 8240–7. Mar 2000. doi:10.1074/jbc.275.11.8240. PMID 10713150. 
  15. ↑ 15.0 15.1 "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain". The Journal of Biological Chemistry 278 (15): 13462–7. Apr 2003. doi:10.1074/jbc.M210483200. PMID 12556468. 
  16. ↑ "Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis". Blood 96 (7): 2574–83. Oct 2000. doi:10.1182/blood.V96.7.2574. PMID 11001914. 
  17. ↑ "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proceedings of the National Academy of Sciences of the United States of America 100 (15): 9011–6. Jul 2003. doi:10.1073/pnas.1431910100. PMID 12853575. Bibcode: 2003PNAS..100.9011M. 
  18. ↑ "A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells". Molecular Biology of the Cell 9 (6): 1437–48. Jun 1998. doi:10.1091/mbc.9.6.1437. PMID 9614185. 

Further reading