STX1A

Syntaxin-1A is a protein that in humans is encoded by the STX1A gene.[5]

STX1A
Identifiers
Aliases	STX1A, HPC-1, P35-1, STX1, SYN1A, syntaxin 1A
External IDs	OMIM: 186590 MGI: 109355 HomoloGene: 37941 GeneCards: STX1A
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q11.23 Start 73,699,206 bp[1] End 73,719,672 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 G2 Start 135,023,482 bp[2] End 135,051,100 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium channel inhibitor activity • ion channel binding • protein N-terminus binding • SNAP receptor activity • kinase binding • chloride channel inhibitor activity • protein heterodimerization activity • SNARE binding • GO:0001948 protein binding • myosin binding • protein domain specific binding • protein binding, bridging • myosin head/neck binding • ATP-dependent protein binding • calcium-dependent protein binding Cellular component • integral component of membrane • cytosol • membrane • synaptic vesicle • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex • voltage-gated potassium channel complex • cell membrane • synapse • synaptic vesicle membrane • secretory granule • extracellular region • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex • cell junction • SNARE complex • intracellular organelle • neuron projection • synaptobrevin 2-SNAP-25-syntaxin-1a complex • actomyosin • cytoplasmic vesicle • presynaptic membrane • GO:0097483, GO:0097481 postsynaptic density • presynaptic active zone membrane • nuclear membrane • integral component of plasma membrane • axon • macromolecular complex • Acrosome • integral component of synaptic vesicle membrane • glutamatergic synapse • integral component of presynaptic membrane • endomembrane system • intracellular • cell Biological process • exocytosis • positive regulation of norepinephrine secretion • synaptic vesicle docking • secretion by cell • regulation of insulin secretion • positive regulation of catecholamine secretion • positive regulation of neurotransmitter secretion • positive regulation of calcium ion-dependent exocytosis • regulation of exocytosis • response to gravity • vesicle docking • positive regulation of excitatory postsynaptic potential • positive regulation of exocytosis • intracellular protein transport • neurotransmitter transport • vesicle-mediated transport • calcium ion regulated exocytosis • regulation of synaptic vesicle priming • protein localization to membrane • modulation of excitatory postsynaptic potential • synaptic vesicle fusion to presynaptic active zone membrane • SNARE complex assembly • cytokine-mediated signaling pathway • synaptic vesicle exocytosis • vesicle fusion • GO:0010554 neurotransmitter secretion • glutamate secretion • protein sumoylation • insulin secretion • regulated exocytosis • hormone secretion • synaptic vesicle endocytosis • Lipid bilayer fusion Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6804	20907
Ensembl	ENSG00000106089	ENSMUSG00000007207
UniProt	Q16623 Q75ME0	O35526
RefSeq (mRNA)	NM_001165903 NM_004603	NM_016801 NM_001359179
RefSeq (protein)	NP_001159375 NP_004594 NP_004594.1	NP_058081 NP_001346108
Location (UCSC)	Chr 7: 73.7 – 73.72 Mb	Chr 5: 135.02 – 135.05 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process.

Syntaxin-1A is a member of the syntaxin superfamily. Syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Syntaxins possess a single C-terminal transmembrane domain, a SNARE [Soluble NSF (N-ethylmaleimide-sensitive fusion protein)-Attachment protein REceptor] domain (known as H3), and an N-terminal regulatory domain (Habc). Syntaxins bind synaptotagmin in a calcium-dependent fashion and interact with voltage dependent calcium and potassium channels via the C-terminal H3 domain. Syntaxin-1A is a key protein in ion channel regulation and synaptic exocytosis.[6]

Clinical significance

Syntaxins serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces explosive exocytosis.[7]

The expression level of STX1A is directly correlated with intelligence in Williams syndrome.[8]

Interactive pathway map

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

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|{{{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

STX1A has been shown to interact with:

• CPLX1,[9][10][11]
• CFTR,[12][13]
• NAPA,[14][15]
• RNF40,[16]
• SCNN1G,[17]
• SLC6A1,[18][19][20]
• SNAP-25,[9][10][14][21][22][23][24][25][26][27][28]
• SNAP23,[26][28][29][30][31]
• STXBP1,[9][14][22][32][33]
• STXBP5,[34][35]
• SYT1[36][37]
• UNC13B,[38]
• VAMP2,[9][10][14][33][39][40] and
• VAMP8.[41]

See also

• Syntaxin

References

1. GRCh38: Ensembl release 89: ENSG00000106089 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000007207 - 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. Bennett MK, Calakos N, Scheller RH (July 1992). "Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones". Science. 257 (5067): 255–9. doi:10.1126/science.1321498. PMID 1321498.
6. "Entrez Gene: STX1A syntaxin 1A (brain)".
7. Zhang R, Maksymowych AB, Simpson LL (July 1995). "Cloning and sequence analysis of a cDNA encoding human syntaxin 1A, a polypeptide essential for exocytosis". Gene. 159 (2): 293–4. doi:10.1016/0378-1119(95)00152-V. PMID 7622072.
8. Gao MC, Bellugi U, Dai L, Mills DL, Sobel EM, Lange K, Korenberg JR (2010). Toland AE (ed.). "Intelligence in Williams Syndrome is related to STX1A, which encodes a component of the presynaptic SNARE complex". PLOS ONE. 5 (4): e10292. doi:10.1371/journal.pone.0010292. PMC 2858212. PMID 20422020. Lay summary – The Salt Lake Tribune.
9. 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". The EMBO Journal. 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. PMC 1171512. PMID 10449403.
10. 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.
11. Hu K, Carroll J, Rickman C, Davletov B (November 2002). "Action of complexin on SNARE complex". The Journal of Biological Chemistry. 277 (44): 41652–6. doi:10.1074/jbc.M205044200. PMID 12200427.
12. Naren AP, Nelson DJ, Xie W, Jovov B, Pevsner J, Bennett MK, Benos DJ, Quick MW, Kirk KL (November 1997). "Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms". Nature. 390 (6657): 302–5. doi:10.1038/36882. PMID 9384384.
13. Cormet-Boyaka E, Di A, Chang SY, Naren AP, Tousson A, Nelson DJ, Kirk KL (September 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. doi:10.1073/pnas.192203899. PMC 129470. PMID 12209004.
14. 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.
15. Hanson PI, Otto H, Barton N, Jahn R (July 1995). "The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin". The Journal of Biological Chemistry. 270 (28): 16955–61. doi:10.1074/jbc.270.28.16955. PMID 7622514.
16. Chin LS, Vavalle JP, Li L (September 2002). "Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation". The Journal of Biological Chemistry. 277 (38): 35071–9. doi:10.1074/jbc.M203300200. PMID 12121982.
17. Berdiev BK, Jovov B, Tucker WC, Naren AP, Fuller CM, Chapman ER, Benos DJ (June 2004). "ENaC subunit-subunit interactions and inhibition by syntaxin 1A". American Journal of Physiology. Renal Physiology. 286 (6): F1100–6. doi:10.1152/ajprenal.00344.2003. PMID 14996668.
18. Beckman ML, Bernstein EM, Quick MW (August 1998). "Protein kinase C regulates the interaction between a GABA transporter and syntaxin 1A". The Journal of Neuroscience. 18 (16): 6103–12. doi:10.1523/JNEUROSCI.18-16-06103.1998. PMC 6793212. PMID 9698305.
19. Quick MW (April 2002). "Substrates regulate gamma-aminobutyric acid transporters in a syntaxin 1A-dependent manner". Proceedings of the National Academy of Sciences of the United States of America. 99 (8): 5686–91. doi:10.1073/pnas.082712899. PMC 122832. PMID 11960023.
20. Deken SL, Beckman ML, Boos L, Quick MW (October 2000). "Transport rates of GABA transporters: regulation by the N-terminal domain and syntaxin 1A". Nature Neuroscience. 3 (10): 998–1003. doi:10.1038/79939. PMID 11017172.
21. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.
22. Hata Y, Südhof TC (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". The Journal of Biological Chemistry. 270 (22): 13022–8. doi:10.1074/jbc.270.22.13022. PMID 7768895.
23. 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". Journal of Cell Science. 113 ( Pt 18) (18): 3197–205. PMID 10954418.
24. Ilardi JM, Mochida S, Sheng ZH (February 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nature Neuroscience. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.
25. Li Y, Chin LS, Weigel C, Li L (November 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". The Journal of Biological Chemistry. 276 (44): 40824–33. doi:10.1074/jbc.M106141200. PMID 11524423.
26. 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". The Journal of Biological Chemistry. 271 (23): 13300–3. doi:10.1074/jbc.271.23.13300. PMID 8663154.
27. 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". The Journal of Biological Chemistry. 269 (44): 27427–32. PMID 7961655.
28. Steegmaier M, Yang B, Yoo JS, Huang B, Shen M, Yu S, Luo Y, Scheller RH (December 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.
29. Imai A, Nashida T, Yoshie S, Shimomura H (August 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.
30. 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.
31. 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. PMID 9168999.
32. Bhaskar K, Shareef MM, Sharma VM, Shetty AP, Ramamohan Y, Pant HC, Raju TR, Shetty KT (January 2004). "Co-purification and localization of Munc18-1 (p67) and Cdk5 with neuronal cytoskeletal proteins". Neurochemistry International. 44 (1): 35–44. doi:10.1016/S0197-0186(03)00099-8. PMID 12963086.
33. Pérez-Brangulí F, Muhaisen A, Blasi J (June 2002). "Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay". Molecular and Cellular Neurosciences. 20 (2): 169–80. doi:10.1006/mcne.2002.1122. PMID 12093152.
34. Widberg CH, Bryant NJ, Girotti M, Rea S, James DE (September 2003). "Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation". The Journal of Biological Chemistry. 278 (37): 35093–101. doi:10.1074/jbc.M304261200. PMID 12832401.
35. Fujita Y, Shirataki H, Sakisaka T, Asakura T, Ohya T, Kotani H, Yokoyama S, Nishioka H, Matsuura Y, Mizoguchi A, Scheller RH, Takai Y (May 1998). "Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process". Neuron. 20 (5): 905–15. doi:10.1016/S0896-6273(00)80472-9. PMID 9620695.
36. Shao X, Li C, Fernandez I, Zhang X, Südhof TC, Rizo J (January 1997). "Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch". Neuron. 18 (1): 133–42. doi:10.1016/S0896-6273(01)80052-0. PMID 9010211.
37. Thomas DM, Ferguson GD, Herschman HR, Elferink LA (July 1999). "Functional and biochemical analysis of the C2 domains of synaptotagmin IV". Molecular Biology of the Cell. 10 (7): 2285–95. doi:10.1091/mbc.10.7.2285. PMC 25443. PMID 10397765.
38. Betz A, Okamoto M, Benseler F, Brose N (January 1997). "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin". The Journal of Biological Chemistry. 272 (4): 2520–6. doi:10.1074/jbc.272.4.2520. PMID 8999968.
39. Margittai M, Otto H, Jahn R (March 1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Letters. 446 (1): 40–4. doi:10.1016/S0014-5793(99)00028-9. PMID 10100611.
40. 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". The Journal of Neuroscience. 17 (5): 1596–603. doi:10.1523/JNEUROSCI.17-05-01596.1997. PMC 6573372. PMID 9030619.
41. Nagamatsu S, Nakamichi Y, Watanabe T, Matsushima S, Yamaguchi S, Ni J, Itagaki E, Ishida H (January 2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". Journal of Cell Science. 114 (Pt 1): 219–227. PMID 11112705.

Further reading

• Peters KW, Qi J, Johnson JP, Watkins SC, Frizzell RA (2002). "Role of snare proteins in CFTR and ENaC trafficking". Pflügers Archiv. 443 Suppl 1: S65–9. doi:10.1007/s004240100647. PMID 11845306.
• Wilson DW, Whiteheart SW, Wiedmann M, Brunner M, Rothman JE (May 1992). "A multisubunit particle implicated in membrane fusion". The Journal of Cell Biology. 117 (3): 531–8. doi:10.1083/jcb.117.3.531. PMC 2289450. PMID 1315316.
• 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.
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External links

• Overview of all the structural information available in the PDB for UniProt: P32851 (Rat Syntaxin-1A) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.