SNAP25

SNAP25
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases SNAP25, CMS18, RIC-4, RIC4, SEC9, SNAP, SNAP-25, bA416N4.2, dJ1068F16.2, SUP, synaptosome associated protein 25kDa, synaptosome associated protein 25
External IDs OMIM: 600322 MGI: 98331 HomoloGene: 13311 GeneCards: SNAP25
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

6616

20614

Ensembl

ENSG00000132639

ENSMUSG00000027273

UniProt

P60880

P60879

RefSeq (mRNA)

NM_011428
NM_001291056

RefSeq (protein)

NP_001277985.1
NP_035558.1

Location (UCSC) Chr 20: 10.22 – 10.31 Mb Chr 2: 136.71 – 136.78 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Synaptosomal-associated protein 25 (SNAP-25) is a t-SNARE protein that is encoded by the SNAP25 gene in humans.[3] SNAP-25 is a component of the trans-SNARE complex, which is proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.[4]

Structure and function

Molecular machinery driving exocytosis in neuromediator release. The core SNARE complex is formed by four α-helices contributed by synaptobrevin, syntaxin and SNAP-25, synaptotagmin serves as a Ca2+ sensor and regulates intimately the SNARE zipping.[5]

SNAP-25, a Q-SNARE protein, is anchored to the cytosolic face of membranes via palmitoyl side chains covalently bound to cysteine amino acid residues in the middle of the molecule. This means that SNAP-25 does not contain a trans-membrane domain.[6]

SNAP-25 has been identified in contributing two α-helices to the SNARE complex, a four-α-helix domain complex.[7] The SNARE complex participates in vesicle fusion, which involves the docking and merging of a vesicle with the cell membrane to bring about an exocytotic event. Synaptobrevin, a protein that is a part of the vesicle-associated membrane protein (VAMP) family, and syntaxin-1 also help form the SNARE complex by each contributing one α-helix. SNAP-25 assembles with synaptobrevin and syntaxin-1 and the selective binding of these proteins enables vesicle docking and fusion to occur at the correct location.[8]

To form the SNARE complex, synaptobrevin, syntaxin-1, and SNAP-25 associate and begin to wrap around each other to form a coiled coil quaternary structure. The α-helices of both synaptobrevin and syntaxin-1 bind to those of SNAP-25. Synaptobrevin binds the α-helix near SNAP-25's C-terminal side, while syntaxin-1 binds the α-helix near the N-terminus.[6]

SNAP-25 inhibits presynaptic P-, Q-, and L-type voltage-gated calcium channels[9] and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion.[10] In glutamatergic synapses, SNAP-25 decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses.[11]

Two isoforms (mRNA splice variants) of SNAP-25 exist, which are labeled A and B. There are nine amino acid residue differences between the two isoforms, including a re-localization of one of the four cysteine residues.[12] The major characteristics of these two forms are outlined in the table below.

SNAP25A SNAP25B
Structure N-terminal α-helix

Random coil linker region with four cysteines clustered towards the center

C-terminal α-helix

N-terminal α-helix

Random coil linker region with four cysteines clustered towards the C-terminus

C-terminal α-helix

Expression Major SNAP-25 isoform in embryos and developing neural tissue

Minimal expression in adult tissue except in pituitary and adrenal gland tissues

Minimal expression during development, major isoform in adult neural tissue[13]
Localization Diffuse Localized to terminals and varicosities[13]

Clinical significance

Consistent with the regulation of synaptic Ca2+ responsiveness, heterozygous deletion of the SNAP-25 gene in mice results in a hyperactive phenotype similar to attention deficit hyperactivity disorder (ADHD). In heterozygous mice, a decrease in hyperactivity is observed with dextroamphetamine (or Dexedrine), an active ingredient in the ADHD drug Adderall. Homozygous deletions of the SNAP-25 gene are lethal. Subsequent studies have suggested that at least some of the SNAP-25 gene mutations in humans might predispose to ADHD.[14][15]

A genome wide association study pointed to the rs362584 polymorphism in the gene as possibly associated with the personality trait neuroticism.[16] Botulinum toxins A, C and E cleave SNAP-25,[17] leading to paralysis in clinically developed botulism.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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NicotineDopaminergic_WP1602 go to article go to article go to article Go to article go to article Go to article Go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article Go to article go to article go to article go to article go to article Go to article Go to article go to article Go to article Go to article Go to article go to article Go to article Go to article Go to article go to article go to article go to article go to article go to article go to article Go to article go to article Go to article Go to article go to article go to article Go to article go to article Go to article Go to article go to article

|{{{bSize}}}px|alt=Nicotine Activity on Dopaminergic Neurons edit]]

Nicotine Activity on Dopaminergic Neurons edit

  1. The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".

Interactions

SNAP-25 has been shown to interact with:

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
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  18. 1 2 3 Chen X, Tomchick DR, Kovrigin E, Araç D, Machius M, Südhof TC, Rizo J (January 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron. 33 (3): 397–409. doi:10.1016/s0896-6273(02)00583-4. PMID 11832227.
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  24. 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 (October 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.
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  26. 1 2 3 4 Ravichandran V, Chawla A, Roche PA (June 1996). "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". J. Biol. Chem. 271 (23): 13300–3. doi:10.1074/jbc.271.23.13300. PMID 8663154.
  27. 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". J. Biol. Chem. 273 (51): 34171–9. doi:10.1074/jbc.273.51.34171. PMID 9852078.
  28. Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, Südhof TC, Rizo J (August 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". EMBO J. 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. PMC 1171512Freely accessible. PMID 10449403.
  29. McMahon HT, Missler M, Li C, Südhof TC (October 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. PMID 7553862.
  30. Gonelle-Gispert C, Molinete M, Halban PA, Sadoul K (September 2000). "Membrane localization and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells". J. Cell. Sci. 113 (18): 3197–205. PMID 10954418.
  31. 1 2 3 Li Y, Chin LS, Weigel C, Li L (November 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". J. Biol. Chem. 276 (44): 40824–33. doi:10.1074/jbc.M106141200. PMID 11524423.
  32. Chapman ER, An S, Barton N, Jahn R (November 1994). "SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils". J. Biol. Chem. 269 (44): 27427–32. PMID 7961655.
  33. Reed GL, Houng AK, Fitzgerald ML (April 1999). "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion". Blood. 93 (8): 2617–26. PMID 10194441.
  34. Gerona RR, Larsen EC, Kowalchyk JA, Martin TF (March 2000). "The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes". J. Biol. Chem. 275 (9): 6328–36. doi:10.1074/jbc.275.9.6328. PMID 10692432.
  35. Zhang X, Kim-Miller MJ, Fukuda M, Kowalchyk JA, Martin TF (May 2002). "Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis". Neuron. 34 (4): 599–611. doi:10.1016/s0896-6273(02)00671-2. PMID 12062043.
  36. Hao JC, Salem N, Peng XR, Kelly RB, Bennett MK (March 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". J. Neurosci. 17 (5): 1596–603. PMID 9030619.

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR000928

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