シナプトブレビン
- 関
- R-SNARE protein
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/08/24 17:55:03」(JST)
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Synaptobrevin |
Three different views of the high resolution structure of a truncated neuronal SNARE complex. Legend: synaptobrevin-2 (red), Syntaxin-1 (pink), SNAP-25 (purple).
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Identifiers |
Symbol |
Synaptobrevin |
Pfam |
PF00957 |
InterPro |
IPR001388 |
PROSITE |
PDOC00368 |
SCOP |
1sfc |
SUPERFAMILY |
1sfc |
OPM superfamily |
218 |
OPM protein |
4wy4 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
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Synaptobrevins (synaptobrevin isotypes 1-2) 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.[1][2][3][4][5]
Synaptobrevin is one of the SNARE proteins involved in formation of the SNARE complexes.
Contents
- 1 Structure
- 2 Function
- 3 Classification
- 4 Clinical significance
- 5 Human proteins containing this domain
- 6 References and notes
- 7 External links
Structure
Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (in neurons).
Function
SNARE proteins are the key components of the molecular machinery that drives fusion of membranes in exocytosis. Their function however is subject to fine-tuning by various regulatory proteins collectively referred to as SNARE masters.
Classification
In the Q/R nomenclature for organizing SNARE proteins, VAMP/synaptobrevin family members are classified as R-SNAREs, so named for the presence of an arginine at a specific location within the primary sequence of the protein (as opposed to the SNAREs of the target membrane, which contain a glutamine and are so named Q-SNAREs). Synaptobrevin is classified as a V-SNARE in the V/T nomenclature, an alternative classification scheme in which SNAREs are classified as V-SNAREs and T-SNAREs for their localization to vesicles and target membranes, respectively.[6]
Clinical significance
Synaptobrevin is degraded by tetanospasmin, a protein derived from the bacterium Clostridium tetani, which causes tetanus. A related bacterium, Clostridium botulinum, produces botulinum toxin that also hydrolyzes synaptobrevin.
Human proteins containing this domain
SEC22A; SEC22B; SYBL1; VAMP1; VAMP2; VAMP3; VAMP4; VAMP5; VAMP8; YKT6;
References and notes
- ^ Baumert M, Maycox PR, Navone F, De Camilli P, Jahn R (February 1, 1989). "Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain". EMBO J. 8 (2): 379–84. PMC 400817 . PMID 2498078.
- ^ Bock JB, Scheller RH (October 1999). "SNARE proteins mediate lipid bilayer fusion". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12227–9. PMC 34255 . PMID 10535902. doi:10.1073/pnas.96.22.12227.
- ^ Ernst JA, Brunger AT (2003). "High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex". J Biol Chem. 278 (10): 8630–6. PMID 12496247. doi:10.1074/jbc.M211889200.
- ^ Fasshauer D, Sutton RB, Brunger AT, Jahn R (December 1998). "Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs". Proc. Natl. Acad. Sci. U.S.A. 95 (26): 15781–6. PMC 28121 . PMID 9861047. doi:10.1073/pnas.95.26.15781.
- ^ Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998). "SNAREpins: minimal machinery for membrane fusion". Cell. 92 (6): 759–72. PMID 9529252. doi:10.1016/S0092-8674(00)81404-X.
- ^ Juan S. Bonifacino and Benjamin S. Glick. "The Mechanisms of Vesicle Budding and Fusion." Cell, Vol. 116, 153–166, January 23, 2004,
External links
- Synaptobrevin at the US National Library of Medicine Medical Subject Headings (MeSH)
Membrane protein: vesicular transport proteins (TC 1F)
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Synaptic vesicle |
SNARE |
Q-SNARE |
- 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 |
- Synaptobrevin/VAMP: VAMP1
- VAMP2
- VAMP3
|
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Synaptotagmin |
- 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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COPI |
- Coatomer
- COPA
- COPB1
- COPB2
- COPD/Archain
- COPE
- COPG
- COPG2
- COPZ1
- COPZ2
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COPII |
- Coatomer
- SEC23A/SEC24A
- SEC13/SEC31
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RME/Clathrin |
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Caveolae |
- Caveolin (CAV1
- CAV2
- CAV3)
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Other/ungrouped |
Vesicle formation |
Adaptor protein complex 1: |
- AP1AR
- AP1B1
- AP1G1
- AP1G2
- AP1M1
- AP1M2
- AP1S1
- AP1S2
- AP1S3
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Adaptor protein complex 2: |
- AP2A1
- AP2A2
- AP2B1
- AP2M1
- AP2S1
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Adaptor protein complex 3: |
- AP3B1
- AP3B2
- AP3D1
- AP3M1
- AP3M2
- AP3S1
- AP3S2
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Adaptor protein complex 4: |
|
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BLOC-1: |
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BLOC-2: |
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BLOC-3: |
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Coats: |
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Small GTPase |
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Other |
- EHD protein family: EHD1
- EHD2
- EHD3
- EHD4
- Vacuolar protein sorting: VPS13B
- VPS33B
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See also vesicular transport protein disorders
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UpToDate Contents
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English Journal
- Phosphatidylserine-Dependent Catalysis of Stalk and Pore Formation by Synaptobrevin JMR-TMD Peptide.
- Tarafdar PK1, Chakraborty H1, Bruno MJ1, Lentz BR2.
- Biophysical journal.Biophys J.2015 Nov 3;109(9):1863-72. doi: 10.1016/j.bpj.2015.08.051.
- Although the importance of a SNARE complex in neurotransmitter release is widely accepted, there exist different views on how the complex promotes fusion. One hypothesis is that the SNARE complex's ability to bring membranes into contact is sufficient for fusion, another points to possible roles of
- PMID 26536263
- Vesicular Synaptobrevin/VAMP2 Levels Guarded by AP180 Control Efficient Neurotransmission.
- Koo SJ1, Kochlamazashvili G1, Rost B2, Puchkov D1, Gimber N1, Lehmann M3, Tadeus G1, Schmoranzer J3, Rosenmund C2, Haucke V4, Maritzen T5.
- Neuron.Neuron.2015 Oct 21;88(2):330-44. doi: 10.1016/j.neuron.2015.08.034. Epub 2015 Sep 24.
- Neurotransmission depends on synaptic vesicle (SV) exocytosis driven by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex formation of vesicular synaptobrevin/VAMP2 (Syb2). Exocytic fusion is followed by endocytic SV membrane retrieval and the high-fidelity reform
- PMID 26412491
- Tissue Plasminogen Activator Expression Is Restricted to Subsets of Excitatory Pyramidal Glutamatergic Neurons.
- Louessard M1, Lacroix A2,3,4, Martineau M5, Mondielli G6, Montagne A1, Lesept F1, Lambolez B2,3,4, Cauli B2,3,4, Mothet JP6, Vivien D7, Maubert E1.
- Molecular neurobiology.Mol Neurobiol.2015 Sep 16. [Epub ahead of print]
- Although the extracellular serine protease tissue plasminogen activator (tPA) is involved in pathophysiological processes such as learning and memory, anxiety, epilepsy, stroke, and Alzheimer's disease, information about its regional, cellular, and subcellular distribution in vivo is lacking. In the
- PMID 26377106
Japanese Journal
- Ca2+-independent syntaxin binding to the C2B effector region of synaptotagmin
- Masumoto Toshio,Suzuki Koichiro,Ohmori Iori,Michiue Hiroyuki,Tomizawa Kazuhito,Fujimura Atsushi,Nishiki Tei-ichi,Matsui Hideki
- Molecular and Cellular Neuroscience 49(1), 1-8, 2012-01
- … SNARE complexes comprising syntaxin 1, 25-kDa synaptosomal-associated protein (SNAP-25), and synaptobrevin 2 were coprecipitzted with synaptotagmin I in the presence of ethylene glycol tetraacetic acid. … Syntaxin, but not SNAP-25 and synaptobrevin, bound to synaptotagmin in a Ca2+-independent manner, and the binding was abolished in the presence of 1 M NaCl. …
- NAID 120005425639
- Factors regulating the abundance and localization of synaptobrevin in the plasma membrane
- DITTMAN J. S.
- Proc. Natl. Acad. Sci. USA 103, 11399-11404, 2006
- NAID 30016238189
- RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding
- KARIM S.
- Biochemical and Biophysical Research Communications 334, 1336-1342, 2005
- NAID 30017846126
Related Links
- Myobloc - Mechanism of Action 3D Medical Animation, AutoFill with Cell Paper recipe applied to a single vesicle and minor overlaps ... The World News (WN) Network, has created this privacy statement in order to demonstrate our ...
- [VAMP; vesicle-associated membrane protein] [synaptobrevin isotypes 1-2] VAMP。VAMP/synaptobrevin familyに含まれる全てのタンパク質は共通の構造をもっていてsと呼ばれる。v- and t-SNAREsに分類されるときは、その合成機関に ...
Related Pictures
★リンクテーブル★
[★]
R-SNAREタンパク質
- 関
- synaptobrevin
[★]
シナプトブレビン1
- 関
- VAMP-1、VAMP1、vesicle-associated membrane protein 1
[★]
シナプトブレビン2
- 関
- VAMP-2、VAMP2、vesicle-associated membrane protein 2
[★]
シナプトブレビン3
- 関
- VAMP3、vesicle-associated membrane protein 3