SNAP-25

SNAP-25 (synaptosome-associated protein of 25,000 daltons) is a membrane bound protein anchored to the cytosolic face of membranes via palmitoyl side chains in the middle of the molecule. SNAP-25 is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin. SNAP-25 inhibits P/Q- and L-type voltage-gated calcium channels located presynaptically cite journal
author = Hodel A
title = SNAP-25
journal = The International Journal of Biochemistry & Cell Biology
volume = 30
issue = 10
pages = 1069–1073
year = 1998
doi = 10.1016/S1357-2725(98)00079-X
] and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion cite journal
author = Chapman ER
title = [http://www.physiology.wisc.edu/chapman/papers/naturereview.pdf Synaptotagmin: A Ca2+ sensor that triggers exocytosis?]
journal = Nature Reviews Molecular Cell Biology
volume = 3
pages = 498–508
year = 2002
] . In glutamatergic synapses SNAP-25 decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses cite journal
author = Pozzi D, Verderio C, Patti L, Grumelli C, Inverardi F, Frassoni C, Bonanno G, Matteoli M
title = [http://dx.doi.org/10.1016/S0896-6273(04)00077-7 SNAP-25 modulation of calcium dynamics underlies differences in GABAergic and glutamatergic responsiveness to depolarization]
journal = Neuron
volume = 41
issue = 4
pages = 599–610
year = 2004
doi = 10.1016/S0896-6273(04)00077-7
] .

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 cite journal
author = Brophy K, Hawi Z, Kirley A, Fitzgerald M, Gill M
title = Synaptosomal-associated protein 25 (SNAP-25) and attention deficit hyperactivity disorder (ADHD): evidence of linkage and association in the Irish population
journal = Molecular Psychiatry
volume = 7
issue = 8
pages = 913–917
year = 2002
doi = 10.1038/sj.mp.4001092
] cite journal
author = Mill J, Curran S, Kent L, Gould A, Huckett L, Richards S, Taylor E, Asherson P
title = Association study of a SNAP-25 microsatellite and attention deficit hyperactivity disorder
journal = American Journal of Medical Genetics
volume = 114
issue = 3
pages = 269–271
year = 2002
doi = 10.1002/ajmg.10253
] .

Botulinum toxins A, C and E cleave SNAP-25 cite journal
author = Aoki KR, Guyer B
title = Botulinum toxin type A and other botulinum toxin serotypes: a comparative review of biochemical and pharmacological actions
journal = European Journal of Neurology
volume = 8
pages = 21–29
year = 2001
doi = 10.1046/j.1468-1331.2001.00035.x
] leading to paralysis in clinically developed botulism.

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hanson PI, Otto H, Barton N, Jahn R |title=The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. |journal=J. Biol. Chem. |volume=270 |issue= 28 |pages= 16955–61 |year= 1995 |pmid= 7622514 |doi=
*cite journal | author=Hata Y, Südhof TC |title=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. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13022–8 |year= 1995 |pmid= 7768895 |doi=
*cite journal | author=Chapman ER, An S, Barton N, Jahn R |title=SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27427–32 |year= 1994 |pmid= 7961655 |doi=
*cite journal | author=Zhao N, Hashida H, Takahashi N, Sakaki Y |title=Cloning and sequence analysis of the human SNAP25 cDNA. |journal=Gene |volume=145 |issue= 2 |pages= 313–4 |year= 1994 |pmid= 8056350 |doi=
*cite journal | author=Bark IC, Wilson MC |title=Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25. |journal=Gene |volume=139 |issue= 2 |pages= 291–2 |year= 1994 |pmid= 8112622 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Maglott DR, Feldblyum TV, Durkin AS, Nierman WC |title=Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p). |journal=Mamm. Genome |volume=7 |issue= 5 |pages= 400–1 |year= 1996 |pmid= 8661740 |doi=
*cite journal | author=Ravichandran V, Chawla A, Roche PA |title=Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13300–3 |year= 1996 |pmid= 8663154 |doi=
*cite journal | author=Rettig J, Sheng ZH, Kim DK, "et al." |title=Isoform-specific interaction of the alpha1A subunits of brain Ca2+ channels with the presynaptic proteins syntaxin and SNAP-25. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 14 |pages= 7363–8 |year= 1996 |pmid= 8692999 |doi=
*cite journal | author=Jagadish MN, Fernandez CS, Hewish DR, "et al." |title=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. |journal=Biochem. J. |volume=317 ( Pt 3) |issue= |pages= 945–54 |year= 1996 |pmid= 8760387 |doi=
*cite journal | author=Betz A, Okamoto M, Benseler F, Brose N |title=Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2520–6 |year= 1997 |pmid= 8999968 |doi=
*cite journal | author=Araki S, Tamori Y, Kawanishi M, "et al." |title=Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c. |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 1 |pages= 257–62 |year= 1997 |pmid= 9168999 |doi= 10.1006/bbrc.1997.6560
*cite journal | author=Lane SR, Liu Y |title=Characterization of the palmitoylation domain of SNAP-25. |journal=J. Neurochem. |volume=69 |issue= 5 |pages= 1864–9 |year= 1997 |pmid= 9349529 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Okamoto M, Südhof TC |title=Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. |journal=J. Biol. Chem. |volume=272 |issue= 50 |pages= 31459–64 |year= 1998 |pmid= 9395480 |doi=
*cite journal | author=Low SH, Roche PA, Anderson HA, "et al." |title=Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3422–30 |year= 1998 |pmid= 9452464 |doi=
*cite journal | author=Poirier MA, Hao JC, Malkus PN, "et al." |title=Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11370–7 |year= 1998 |pmid= 9556632 |doi=
*cite journal | author=Prekeris R, Klumperman J, Chen YA, Scheller RH |title=Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. |journal=J. Cell Biol. |volume=143 |issue= 4 |pages= 957–71 |year= 1998 |pmid= 9817754 |doi=
*cite journal | author=Gonelle-Gispert C, Halban PA, Niemann H, "et al." |title=SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion. |journal=Biochem. J. |volume=339 ( Pt 1) |issue= |pages= 159–65 |year= 1999 |pmid= 10085240 |doi=
*cite journal | author=Ilardi JM, Mochida S, Sheng ZH |title=Snapin: a SNARE-associated protein implicated in synaptic transmission. |journal=Nat. Neurosci. |volume=2 |issue= 2 |pages= 119–24 |year= 1999 |pmid= 10195194 |doi= 10.1038/5673

External links

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