SNAP23

Last updated
SNAP23
Protein SNAP23 PDB 1nhl.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SNAP23 , HsT17016, SNAP-23, SNAP23A, SNAP23B, synaptosome associated protein 23kDa, synaptosome associated protein 23
External IDs OMIM: 602534 MGI: 109356 HomoloGene: 37857 GeneCards: SNAP23
Orthologs
SpeciesHumanMouse
Entrez

8773

20619

Ensembl

ENSG00000092531

ENSMUSG00000027287

UniProt

O00161

O09044

RefSeq (mRNA)

NM_003825
NM_130798

NM_001177792
NM_001177793
NM_009222

RefSeq (protein)

NP_003816
NP_570710

NP_001171263
NP_001171264
NP_033248

Location (UCSC) Chr 15: 42.49 – 42.55 Mb Chr 2: 120.4 – 120.43 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. [5] [6] Two alternative transcript variants encoding different protein isoforms have been described for this gene.

Contents

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. [7]

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:

Related Research Articles

<span class="mw-page-title-main">SNARE protein</span> Protein family

SNARE proteins – "SNAPREceptors" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments. The best studied SNAREs are those that mediate the release of synaptic vesicles containing neurotransmitters in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.

<span class="mw-page-title-main">Synaptobrevin</span>

Synaptobrevins are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family.

<span class="mw-page-title-main">SNAP25</span> Protein-coding gene in the species Homo sapiens

Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.

<span class="mw-page-title-main">STX1A</span> Protein-coding gene in the species Homo sapiens

Syntaxin-1A is a protein that in humans is encoded by the STX1A gene.

<span class="mw-page-title-main">STX4</span> Protein-coding gene in the species Homo sapiens

Syntaxin-4 is a protein that in humans is encoded by the STX4 gene.

<span class="mw-page-title-main">SYT1</span> Protein-coding gene in the species Homo sapiens

Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.

<span class="mw-page-title-main">VAMP2</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.

<span class="mw-page-title-main">Vesicle-associated membrane protein 7</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 7 (VAMP-7), is a protein that in humans is encoded by the VAMP7 gene also known as the or SYBL1 gene.

<span class="mw-page-title-main">STX7</span> Human protein and coding gene

Syntaxin-7 is a protein that in humans is encoded by the STX7 gene.

<span class="mw-page-title-main">STX6</span> Protein-coding gene in the species Homo sapiens

Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.

<span class="mw-page-title-main">NAPA (gene)</span> Protein-coding gene in the species Homo sapiens

N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.

<span class="mw-page-title-main">VAMP3</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.

<span class="mw-page-title-main">STX2</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">Vesicle-associated membrane protein 8</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene.

<span class="mw-page-title-main">SNAP29</span> Protein-coding gene in the species Homo sapiens

Synaptosomal-associated protein 29 is a protein that in humans is encoded by the SNAP29 gene.

<span class="mw-page-title-main">VAMP4</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 4 is a protein that in humans is encoded by the VAMP4 gene.

<span class="mw-page-title-main">VAMP1</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 1 (VAMP1) is a protein that in humans is encoded by the VAMP1 gene.

<span class="mw-page-title-main">Syntaxin 3</span> Protein-coding gene in the species Homo sapiens

Syntaxin 3, also known as STX3, is a protein which in humans is encoded by the STX3 gene.

Munc-18 proteins are the mammalian homologue of UNC-18 and are a member of the Sec1/Munc18-like (SM) protein family. Munc-18 proteins have been identified as essential components of the synaptic vesicle fusion protein complex and are crucial for the regulated exocytosis of neurons and neuroendocrine cells.

<span class="mw-page-title-main">SNAP47</span>

Synaptosome-associated protein, 47 kDal (SNAP47) is a human protein encoded by the SNAP47 gene. Other aliases of this gene are SVAP1, HEL170, ESFI5812, and HEL-S-290. SNAP47 is a synaptosome protein which is associated with the protein coding in multiple diseases, including non small cell lung cancer and schizophrenia. SNAP47 is a member of the SNAP protein family. SNAP proteins are t-snare proteins that are a component of SNARE complex. The SNARE complex mediates vesicle fusion by creating tight complex that brings vesicle and membrane together. This protein causes ubiquitous expression in testis, ovary, and many other tissues

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000092531 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027287 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Mollinedo F, Lazo PA (Feb 1997). "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. doi:10.1006/bbrc.1997.6196. PMID   9070898.
  6. 1 2 3 4 5 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.
  7. ↑ "Entrez Gene: SNAP23 synaptosomal-associated protein, 23kDa".
  8. ↑ Cormet-Boyaka E, Di A, Chang SY, Naren AP, Tousson A, Nelson DJ, Kirk KL (Sep 2002). "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. Bibcode:2002PNAS...9912477C. doi: 10.1073/pnas.192203899 . PMC   129470 . PMID   12209004.
  9. ↑ Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (Dec 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry. 41 (50): 14906–15. doi:10.1021/bi026417u. PMID   12475239.
  10. 1 2 Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
  11. ↑ Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T (Oct 2003). "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. doi:10.1042/BJ20030427. PMC   1223698 . PMID   12877659.
  12. ↑ Valdez AC, Cabaniols JP, Brown MJ, Roche PA (Mar 1999). "Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network". Journal of Cell Science. 112 (6): 845–54. doi:10.1242/jcs.112.6.845. PMID   10036234.
  13. 1 2 3 4 5 6 7 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.
  14. 1 2 3 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.
  15. 1 2 3 4 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. hdl: 20.500.14094/D2002245 . PMID   9168999.
  16. 1 2 3 Steegmaier M, Yang B, Yoo JS, Huang B, Shen M, Yu S, Luo Y, Scheller RH (Dec 1998). "Three novel proteins of the syntaxin/SNAP-25 family". The Journal of Biological Chemistry. 273 (51): 34171–9. doi: 10.1074/jbc.273.51.34171 . PMID   9852078.
  17. 1 2 3 4 Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (Jun 2000). "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. doi: 10.4049/jimmunol.164.11.5850 . PMID   10820264.
  18. 1 2 Kawanishi M, Tamori Y, Okazawa H, Araki S, Shinoda H, Kasuga M (Mar 2000). "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. doi: 10.1074/jbc.275.11.8240 . PMID   10713150.
  19. 1 2 Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ (Apr 2003). "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain". The Journal of Biological Chemistry. 278 (15): 13462–7. doi: 10.1074/jbc.M210483200 . PMID   12556468.
  20. ↑ Martín-Martín B, Nabokina SM, Blasi J, Lazo PA, Mollinedo F (Oct 2000). "Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis". Blood. 96 (7): 2574–83. doi:10.1182/blood.V96.7.2574. PMID   11001914.
  21. ↑ Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, Daviet L, Formstecher E, Hamburger A, Filippini F, D'Esposito M, Galli T (Jul 2003). "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. Bibcode:2003PNAS..100.9011M. doi: 10.1073/pnas.1431910100 . PMC   166429 . PMID   12853575.
  22. ↑ Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, Niemann H, Louvard D (Jun 1998). "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. doi:10.1091/mbc.9.6.1437. PMC   25366 . PMID   9614185.

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