WordNet
- put in play with a snap; "snap a football"
- break suddenly and abruptly, as under tension; "The pipe snapped" (同)crack
- a spell of cold weather; "a cold snap in the middle of May"
- close with a snapping motion; "The lock snapped shut"
- a fastener used on clothing; fastens with a snapping sound; "children can manage snaps better than buttons" (同)snap fastener, press stud
- the act of snapping the fingers; movement of a finger from the tip to the base of the thumb on the same hand; "he gave his fingers a snap"
- a sudden breaking
- the noise produced by the rapid movement of a finger from the tip to the base of the thumb on the same hand; "servants appeared at the snap of his fingers"
- move or strike with a noise; "he clicked on the light"; "his arm was snapped forward" (同)click
- cause to make a snapping sound; "snap your fingers" (同)click, flick
- make a sharp sound; "his fingers snapped" (同)crack
- utter in an angry, sharp, or abrupt tone; "The sales clerk snapped a reply at the angry customer"; "The guard snarled at us" (同)snarl
- bring the jaws together; "he snapped indignantly"
- move with a snapping sound; "bullets snapped past us"
PrepTutorEJDIC
- 『パチン』(『ポキン』,『カチッ』,『ピシッ』)『と音をたてる』・〈木の枝などが〉『ポキッと折れる』,〈糸などが〉プツンと切れる・〈戸・ふた・カギなどが〉パチン(カチッなど)と音をたてて(…の状態に)なる《+『形』〈補〉》・(…に)ぱくっとかみつく《+『at』+『名』》・…‘を'『パチン(ピシッ)と音をさせる』・…‘を'ポキッと折る,プツンと切る;…‘を'パチッと締める・〈命令・応答など〉‘を'ピシッと言う《+『out』+『名,』+『名』+『out』》・《話》〈スナップ写真〉‘を'撮る・〈C〉『ポキッと折れる音』,プツンと切れる音;ビシャッと閉まる音・〈C〉(衣服などの)『スナップ』,留め金 / 〈C〉ぱっと飛びつくこと(かみつくこと,ひっつかむこと) ・〈C〉(急に襲う)一時の寒気・〈C〉(薄くてぱりぱりとした)ショウガ入りクッキー・=snapshot・〈U〉《話》活気,精力・〈C〉《単数形で》《話》容易なこと,楽な仕事・《話》即座の,急になされた・《話》容易な,楽な・どんぴしゃり,バッチリ
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/06/21 21:58:40」(JST)
[Wiki en表示]
Synaptosomal-associated protein, 25kDa |
PDB rendering based on 1jth. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1KIL, 1XTG, 3DDA, 3DDB, 3RK2, 3RK3, 3RL0
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Identifiers |
Symbols |
SNAP25; RIC-4; RIC4; SEC9; SNAP; SNAP-25; bA416N4.2; dJ1068F16.2 |
External IDs |
OMIM: 600322 MGI: 98331 HomoloGene: 13311 GeneCards: SNAP25 Gene |
Gene Ontology |
Molecular function |
• SNARE binding
• protein binding
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Cellular component |
• cytoplasm
• trans-Golgi network
• plasma membrane
• membrane
• cell junction
• growth cone
• BLOC-1 complex
• SNARE complex
• neuron projection
• synapse
• perinuclear region of cytoplasm
• synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex
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Biological process |
• neurotransmitter uptake
• energy reserve metabolic process
• synaptic transmission
• neurotransmitter secretion
• glutamate secretion
• synaptic vesicle docking involved in exocytosis
• small molecule metabolic process
• regulation of insulin secretion
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
6616 |
20614 |
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Ensembl |
ENSG00000132639 |
ENSMUSG00000027273 |
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UniProt |
P60880 |
P60879 |
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RefSeq (mRNA) |
NM_003081 |
NM_011428 |
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RefSeq (protein) |
NP_003072 |
NP_035558 |
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Location (UCSC) |
Chr 20:
10.2 – 10.29 Mb |
Chr 2:
136.71 – 136.78 Mb |
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PubMed search |
[1] |
[2] |
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Synaptosomal-associated protein 25 (SNAP-25) is a t-SNARE protein that is encoded by the SNAP25 gene in humans.[1] 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.[2]
Contents
- 1 Structure and function
- 2 Clinical significance
- 3 Interactive pathway map
- 4 Interactions
- 5 References
- 6 Further reading
- 7 External links
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Structure and function[edit]
SNAP-25 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[3] and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion.[4] In glutamatergic synapses SNAP-25 decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses.[5]
SNAP-25 family |
Structure of a SNARE complex involved in synaptic exocytosis. |
Identifiers |
Symbol |
SNAP-25 |
Pfam |
PF00835 |
InterPro |
IPR000928 |
SCOP |
1sfc |
SUPERFAMILY |
1sfc |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe |
PDBsum |
structure summary |
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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 Ca 2+ sensor and regulates intimately the SNARE zipping. [6]
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Clinical significance[edit]
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.[7][8]
A genome wide association study pointed to the rs362584 polymorphism in the gene as possibly associated with the personality trait neuroticism.[9] Botulinum toxins A, C and E cleave SNAP-25[10] leading to paralysis in clinically developed botulism.
Interactive pathway map[edit]
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
Nicotine Activity on Dopaminergic Neurons edit
- ^ The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".
Interactions[edit]
SNAP-25 has been shown to interact with STX4,[11][12][13][14] STX2,[11][12] Syntaxin 3,[11][12][14] STX1A,[11][12][14][15][16][17][18][19][20][21][22] KIF5B,[23] TRIM9,[20] STX11,[15][24] CPLX1,[22][25] SYT1,[26][27] VAMP2,[20][22][28] SNAPAP[19] and ITSN1.[29]
References[edit]
- ^ Maglott DR, Feldblyum TV, Durkin AS, Nierman WC (May 1996). "Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p)". Mamm. Genome 7 (5): 400–1. doi:10.1007/s003359900120. PMID 8661740.
- ^ Sudhof TC, Rizo J (2002). "Snares and Munc18 in synaptic vesicle fusion". Nat Rev Neurosci 3 (8): 641–653. doi:10.1038/nrn898. PMID 12154365.
- ^ Hodel A (October 1998). "SNAP-25". Int. J. Biochem. Cell Biol. 30 (10): 1069–73. doi:10.1016/S1357-2725(98)00079-X. PMID 9785471.
- ^ Chapman ER (July 2002). "Synaptotagmin: a Ca(2+) sensor that triggers exocytosis?". Nat. Rev. Mol. Cell Biol. 3 (7): 498–508. doi:10.1038/nrm855. PMID 12094216. [dead link]
- ^ Verderio C, Pozzi D, Pravettoni E, Inverardi F, Schenk U, Coco S, Proux-Gillardeaux V, Galli T, Rossetto O, Frassoni C, Matteoli M (February 2004). "SNAP-25 modulation of calcium dynamics underlies differences in GABAergic and glutamatergic responsiveness to depolarization". Neuron 41 (4): 599–610. doi:10.1016/S0896-6273(04)00077-7. PMID 14980208.
- ^ Georgiev, Danko D .; James F . Glazebrook (2007). "Subneuronal processing of information by solitary waves and stochastic processes". In Lyshevski, Sergey Edward. Nano and Molecular Electronics Handbook. Nano and Microengineering Series. CRC Press. pp. 17–1–17–41. ISBN 978-0-8493-8528-5.
- ^ Brophy K, Hawi Z, Kirley A, Fitzgerald M, Gill M (2002). "Synaptosomal-associated protein 25 (SNAP-25) and attention deficit hyperactivity disorder (ADHD): evidence of linkage and association in the Irish population". Mol. Psychiatry 7 (8): 913–7. doi:10.1038/sj.mp.4001092. PMID 12232787.
- ^ Mill J, Curran S, Kent L, Gould A, Huckett L, Richards S, Taylor E, Asherson P (April 2002). "Association study of a SNAP-25 microsatellite and attention deficit hyperactivity disorder". Am. J. Med. Genet. 114 (3): 269–71. doi:10.1002/ajmg.10253. PMID 11920846.
- ^ Terracciano A, Sanna S, Uda M, Deiana B, Usala G, Busonero F, Maschio A, Scally M, Patriciu N, Chen WM, Distel MA, Slagboom EP, Boomsma DI, Villafuerte S, Sliwerska E, Burmeister M, Amin N, Janssens AC, van Duijn CM, Schlessinger D, Abecasis GR, Costa PT (October 2008). "Genome-wide association scan for five major dimensions of personality". Mol. Psychiatry 15 (6): 647–56. doi:10.1038/mp.2008.113. PMC 2874623. PMID 18957941.
- ^ Aoki KR, Guyer B (November 2001). "Botulinum toxin type A and other botulinum toxin serotypes: a comparative review of biochemical and pharmacological actions". Eur. J. Neurol. 8 Suppl 5: 21–9. doi:10.1046/j.1468-1331.2001.00035.x. PMID 11851731.
- ^ a b c d Hata, Y; Südhof T C (June 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". J. Biol. Chem. (UNITED STATES) 270 (22): 13022–8. doi:10.1074/jbc.270.22.13022. ISSN 0021-9258. PMID 7768895.
- ^ a b c d Ravichandran, V; Chawla A, Roche P A (June 1996). "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". J. Biol. Chem. (UNITED STATES) 271 (23): 13300–3. doi:10.1074/jbc.271.23.13300. ISSN 0021-9258. PMID 8663154.
- ^ Reed, G L; Houng A K, Fitzgerald M L (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 (UNITED STATES) 93 (8): 2617–26. ISSN 0006-4971. PMID 10194441.
- ^ a b c Steegmaier, M; Yang B, Yoo J S, Huang B, Shen M, Yu S, Luo Y, Scheller R H (Dec. 1998). "Three novel proteins of the syntaxin/SNAP-25 family". J. Biol. Chem. (UNITED STATES) 273 (51): 34171–9. doi:10.1074/jbc.273.51.34171. ISSN 0021-9258. PMID 9852078.
- ^ a b Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070.
- ^ Dulubova, I; Sugita S, Hill S, Hosaka M, Fernandez I, Südhof T C, Rizo J (August 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". EMBO J. (ENGLAND) 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. ISSN 0261-4189. PMC 1171512. PMID 10449403.
- ^ McMahon, H T; Missler M, Li C, Südhof T C (October 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell (UNITED STATES) 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. ISSN 0092-8674. PMID 7553862.
- ^ Gonelle-Gispert, C; Molinete M, Halban P A, Sadoul K (September 2000). "Membrane localization and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells". J. Cell. Sci. (ENGLAND) 113 (18): 3197–205. ISSN 0021-9533. PMID 10954418.
- ^ a b Ilardi, J M; Mochida S, Sheng Z H (February 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nat. Neurosci. (UNITED STATES) 2 (2): 119–24. doi:10.1038/5673. ISSN 1097-6256. PMID 10195194.
- ^ a b c Li, Y; Chin L S, Weigel C, Li L (November 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". J. Biol. Chem. (United States) 276 (44): 40824–33. doi:10.1074/jbc.M106141200. ISSN 0021-9258. PMID 11524423.
- ^ Chapman, E R; 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. (UNITED STATES) 269 (44): 27427–32. ISSN 0021-9258. PMID 7961655.
- ^ a b c Chen, Xiaocheng; Tomchick Diana R, Kovrigin Evguenii, Araç Demet, Machius Mischa, Südhof Thomas C, Rizo Josep (January 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron (United States) 33 (3): 397–409. doi:10.1016/S0896-6273(02)00583-4. ISSN 0896-6273. PMID 11832227.
- ^ Diefenbach, Russell J; Diefenbach Eve, Douglas Mark W, Cunningham Anthony L (Dec. 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry (United States) 41 (50): 14906–15. doi:10.1021/bi026417u. ISSN 0006-2960. PMID 12475239.
- ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ^ Hu, Kuang; Carroll Joe, Rickman Colin, Davletov Bazbek (November 2002). "Action of complexin on SNARE complex". J. Biol. Chem. (United States) 277 (44): 41652–6. doi:10.1074/jbc.M205044200. ISSN 0021-9258. PMID 12200427.
- ^ Gerona, R R; Larsen E C, Kowalchyk J A, Martin T F (March 2000). "The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes". J. Biol. Chem. (UNITED STATES) 275 (9): 6328–36. doi:10.1074/jbc.275.9.6328. ISSN 0021-9258. PMID 10692432.
- ^ Zhang, Xiaodong; Kim-Miller Mindy J, Fukuda Mitsunori, Kowalchyk Judith A, Martin Thomas F J (May 2002). "Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis". Neuron (United States) 34 (4): 599–611. doi:10.1016/S0896-6273(02)00671-2. ISSN 0896-6273. PMID 12062043.
- ^ Hao, J C; Salem N, Peng X R, Kelly R B, Bennett M K (March 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". J. Neurosci. (UNITED STATES) 17 (5): 1596–603. ISSN 0270-6474. PMID 9030619.
- ^ Okamoto, M; Schoch S, Südhof T C (June 1999). "EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin and SNAP-25. A protein connection between exocytosis and endocytosis?". J. Biol. Chem. (UNITED STATES) 274 (26): 18446–54. doi:10.1074/jbc.274.26.18446. ISSN 0021-9258. PMID 10373452.
Further reading[edit]
- Hanson PI, Otto H, Barton N, Jahn R (1995). "The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin.". J. Biol. Chem. 270 (28): 16955–61. doi:10.1074/jbc.270.28.16955. PMID 7622514.
- Hata Y, Südhof TC (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.". J. Biol. Chem. 270 (22): 13022–8. doi:10.1074/jbc.270.22.13022. PMID 7768895.
- Chapman ER, An S, Barton N, Jahn R (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.
- Zhao N, Hashida H, Takahashi N, Sakaki Y (1994). "Cloning and sequence analysis of the human SNAP25 cDNA.". Gene 145 (2): 313–4. doi:10.1016/0378-1119(94)90027-2. PMID 8056350.
- Bark IC, Wilson MC (1994). "Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25.". Gene 139 (2): 291–2. doi:10.1016/0378-1119(94)90773-0. PMID 8112622.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Maglott DR, Feldblyum TV, Durkin AS, Nierman WC (1996). "Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p).". Mamm. Genome 7 (5): 400–1. doi:10.1007/s003359900120. PMID 8661740.
- Ravichandran V, Chawla A, Roche PA (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.
- Rettig J, Sheng ZH, Kim DK, et al. (1996). "Isoform-specific interaction of the alpha1A subunits of brain Ca2+ channels with the presynaptic proteins syntaxin and SNAP-25.". Proc. Natl. Acad. Sci. U.S.A. 93 (14): 7363–8. doi:10.1073/pnas.93.14.7363. PMC 38990. PMID 8692999.
- Jagadish MN, Fernandez CS, Hewish DR, et al. (1996). "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.". Biochem. J. 317 (3): 945–54. PMC 1217577. PMID 8760387.
- Betz A, Okamoto M, Benseler F, Brose N (1997). "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin.". J. Biol. Chem. 272 (4): 2520–6. doi:10.1074/jbc.272.4.2520. PMID 8999968.
- Araki S, Tamori Y, Kawanishi M, et al. (1997). "Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c.". Biochem. Biophys. Res. Commun. 234 (1): 257–62. doi:10.1006/bbrc.1997.6560. PMID 9168999.
- Lane SR, Liu Y (1997). "Characterization of the palmitoylation domain of SNAP-25.". J. Neurochem. 69 (5): 1864–9. doi:10.1046/j.1471-4159.1997.69051864.x. PMID 9349529.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Okamoto M, Südhof TC (1998). "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis.". J. Biol. Chem. 272 (50): 31459–64. doi:10.1074/jbc.272.50.31459. PMID 9395480.
- Low SH, Roche PA, Anderson HA, et al. (1998). "Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells.". J. Biol. Chem. 273 (6): 3422–30. doi:10.1074/jbc.273.6.3422. PMID 9452464.
- Poirier MA, Hao JC, Malkus PN, et al. (1998). "Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure.". J. Biol. Chem. 273 (18): 11370–7. doi:10.1074/jbc.273.18.11370. PMID 9556632.
- Prekeris R, Klumperman J, Chen YA, Scheller RH (1998). "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes.". J. Cell Biol. 143 (4): 957–71. doi:10.1083/jcb.143.4.957. PMC 2132958. PMID 9817754.
- Gonelle-Gispert C, Halban PA, Niemann H, et al. (1999). "SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion.". Biochem. J. 339 (1): 159–65. doi:10.1042/0264-6021:3390159. PMC 1220140. PMID 10085240.
- Ilardi JM, Mochida S, Sheng ZH (1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission.". Nat. Neurosci. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.
External links[edit]
- SNAP25 Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
PDB gallery
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1jth: Crystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a
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1kil: Three-dimensional structure of the complexin/SNARE complex
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1n7s: High Resolution Structure of a Truncated Neuronal SNARE Complex
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1sfc: NEURONAL SYNAPTIC FUSION COMPLEX
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1urq: CRYSTAL STRUCTURE OF NEURONAL Q-SNARES IN COMPLEX WITH R-SNARE MOTIF OF TOMOSYN
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1xtg: Crystal structure of NEUROTOXIN BONT/A complexed with Synaptosomal-associated protein 25
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Membrane protein: vesicular transport proteins (TC 1F)
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Synaptic vesicle |
SNARE
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Q-SNARE
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SNAP25 · SNAP29
Syntaxin (STX1A, STX1B, STX2, STX3, STX4, STX5, STX6, STX7, STX8, STX10, STX11, STX12, STX16, STX17, STX18, STX19)
Munc-18: STXBP1 · STXBP2 · STXBP3 · STXBP4 · STXBP5 · STXBP6
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R-SNARE
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Synaptobrevin/VAMP: VAMP1 · VAMP2 · VAMP3
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Synaptotagmin
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SYT1 · SYT2 · SYT3 · SYT4 · SYT5 · SYT6 · SYT7 · SYT8 · SYT9 · SYT10 · SYT11 · SYT12 · SYT13 · SYT14 · SYT15 · SYT16 · SYT17
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Other
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Synaptophysin · Synapsin
Small GTPase: RAB3A
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COPI |
Coatomer (COPA, COPB1, COPB2, COPE, COPG, COPG2, COPZ1, COPZ2)
Archain
Small GTPase: ARF
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COPII |
Vesicle formation: SEC23A
Small GTPase: SAR1A
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RME/Clathrin |
CLTA · CLTB · CLTC
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Caveolae |
Caveolin (CAV1 · CAV2 · CAV3)
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Other/ungrouped |
Vesicle formation
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Adaptor protein complex 1: AP1AR · AP1B1 · AP1G1 · AP1G2 · AP1M1 · AP1M2 · AP1S1 · AP1S2 · AP1S3
Adaptor protein complex 2: AP2A1 · AP2A2 · AP2B1 · AP2M1 · AP2S1
Adaptor protein complex 3: AP3B1 · AP3B2 · AP3D1 · AP3M1 · AP3M2 · AP3S1 · AP3S2
Adaptor protein complex 4: AP4B1 · AP4E1 · AP4M1 · AP4S1
LMAN1
LYST
BLOC-1: DTNBP1 · BLOC153
BLOC-2: HPS3 · HPS5 · HPS6
BLOC-3: HPS1 · HPS4
Coats: Retromer · TIP47
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Small GTPase
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Dynamin (DNM1, DNM2, DNM3)
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Other
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EHD protein family: EHD1 · EHD2 · EHD3 · EHD4
Sorting nexins
vacuolar protein sorting: VPS13B · VPS33B
SYNRG
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see also vesicular transport protein disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr
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This article incorporates text from the public domain Pfam and InterPro IPR000928
UpToDate Contents
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English Journal
- Alzheimer's disease and type 2 diabetes-related alterations in brain mitochondria, autophagy and synaptic markers.
- Carvalho C1, Santos MS2, Oliveira CR3, Moreira PI4.
- Biochimica et biophysica acta.Biochim Biophys Acta.2015 Aug;1852(8):1665-75. doi: 10.1016/j.bbadis.2015.05.001. Epub 2015 May 7.
- We aimed to investigate mitochondrial function, biogenesis and autophagy in the brain of type 2 diabetes (T2D) and Alzheimer's disease (AD) mice. Isolated brain mitochondria and homogenates from cerebral cortex and hippocampus of wild-type (WT), triple transgenic AD (3xTg-AD) and T2D mice were used
- PMID 25960150
- Enhanced detection of type C botulinum neurotoxin by the Endopep-MS assay through optimization of peptide substrates.
- Wang D1, Krilich J1, Baudys J1, Barr JR1, Kalb SR2.
- Bioorganic & medicinal chemistry.Bioorg Med Chem.2015 Jul 1;23(13):3667-73. doi: 10.1016/j.bmc.2015.04.012. Epub 2015 Apr 10.
- It is essential to have a simple, quick and sensitive method for the detection and quantification of botulinum neurotoxins, the most toxic substances and the causative agents of botulism. Type C botulinum neurotoxin (BoNT/C) represents one of the seven members of distinctive BoNT serotypes (A to G)
- PMID 25913863
Japanese Journal
- A Single Amino Acid Mutation in SNAP-25 Induces Anxiety-Related Behavior in Mouse
- Kataoka Masakazu,Yamamori Saori,Suzuki Eiji,Watanabe Shigeru,Sato Taku,Miyaoka Hitoshi,Azuma Sadahiro,Ikegami Shiro,Kuwahara Reiko,Suzuki-Migishima Rika,Nakahara Yohko,Nihonmatsu Itsuko,Inokuchi Kaoru,Katoh-Fukui Yuko,Yokoyama Minesuke,Takahashi Masami
- PLOS ONE 6(9), 2011-09-20
- … Synaptosomal-associated protein of 25 kDa (SNAP-25) is a presynaptic protein essential for neurotransmitter release. … Previously, we demonstrate that protein kinase C (PKC) phosphorylates Ser(187) of SNAP-25, and enhances neurotransmitter release by recruiting secretory vesicles near to the plasma membrane. …
- NAID 120004664532
Related Links
- み込み,Ca チャンネルやK チャンネルの機能制御などの 多様な機能に関わる可能性が明らかとなっている. SNAP-25は脳と内分泌細胞に発現しているが,エクソ ン5の違いによるスプライシングアイソフォーム(a とb) が存在する2) ...
- バニキンズ,ローズオニールキューピー,ワグナー社トイアニマル,ベークライトボタン,ボンゾ,アトウェル,ビスクドール,,ベークライトアクセサリー,シルバーアクセサリー,セルロイド,小さくてもいつもそばにいてほしいちょっと雰囲気 ...
Related Pictures
★リンクテーブル★
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黒質
- 関
- nigra、nigral、substantia nigra
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