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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/09/11 18:55:29」(JST)

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Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.^[1]^[2]

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.^[2]

Interactions[edit source | edit]

VAMP3 has been shown to interact with

BCAP31,^[3]
BVES,^[4]
SNAP23,^[5]^[6]^[7]
STX4,^[5]^[6]^[8]^[9]
STX6.^[10]

References[edit source | edit]

^ Bernstein AM, Whiteheart SW (Apr 1999). "Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets". Blood 93 (2): 571–9. PMID 9885218.
^ ^a ^b "Entrez Gene: VAMP3 vesicle-associated membrane protein 3 (cellubrevin)".
^ Annaert WG, Becker B, Kistner U, Reth M, Jahn R (December 1997). "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31". J. Cell Biol. 139 (6): 1397–410. doi:10.1083/jcb.139.6.1397. PMC 2132629. PMID 9396746.
^ Hager HA, Roberts RJ, Cross EE, Proux-Gillardeaux V, Bader DM (February 2010). "Identification of a novel Bves function: regulation of vesicular transport". EMBO J. 29 (3): 532–45. doi:10.1038/emboj.2009.379. PMC 2830705. PMID 20057356.
^ ^a ^b 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". Arch. Oral Biol. 48 (8): 597–604. doi:10.1016/S0003-9969(03)00116-X. PMID 12828989.
^ ^a ^b Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (June 2000). "Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment". J. Immunol. 164 (11): 5850–7. PMID 10820264.
^ Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ (April 2003). "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain". J. Biol. Chem. 278 (15): 13462–7. doi:10.1074/jbc.M210483200. PMID 12556468.
^ 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. doi:10.1038/nature04209. PMID 16189514.
^ Polgár J, Chung SH, Reed GL (August 2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood 100 (3): 1081–3. doi:10.1182/blood.V100.3.1081. PMID 12130530.
^ Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L (February 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". J. Cell Biol. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.

English Journal

ATG16L1 meets ATG9 in recycling endosomes: Additional roles for the plasma membrane and endocytosis in autophagosome biogenesis.

Puri C, Renna M, Bento CF, Moreau K, Rubinsztein DC.Author information Department of Medical Genetics; Cambridge Institute for Medical Research; University of Cambridge; Cambridge UK.AbstractAutophagosomes are formed by double-membraned structures, which engulf portions of cytoplasm. Autophagosomes ultimately fuse with lysosomes, where their contents are degraded. The origin of the autophagosome membrane may involve different sources, such as mitochondria, Golgi, endoplasmic reticulum, plasma membrane, and recycling endosomes. We recently observed that ATG9 localizes on the plasma membrane in clathrin-coated structures and is internalized following a classical endocytic pathway through early and then recycling endosomes. By contrast, ATG16L1 is also internalized by clathrin-mediated endocytosis but via different clathrin-coated pits, and appears to follow a different route to the recycling endosomes. The R-SNARE VAMP3 mediates the coalescence of the 2 different pools of vesicles (containing ATG16L1 or ATG9) in recycling endosomes. The heterotypic fusion between ATG16L1- and ATG9-containing vesicles strongly correlates with subsequent autophagosome formation. Thus, ATG9 and ATG16L1 both traffic from the plasma membrane to autophagic precursor structures and provide 2 routes from the plasma membrane to autophagosomes.
Autophagy.Autophagy.2014 Jan 1;10(1):182-184. Epub 2013 Nov 19.
Autophagosomes are formed by double-membraned structures, which engulf portions of cytoplasm. Autophagosomes ultimately fuse with lysosomes, where their contents are degraded. The origin of the autophagosome membrane may involve different sources, such as mitochondria, Golgi, endoplasmic reticulum,
PMID 24257061

Vesicular transport system in myotubes: ultrastructural study and signposting with vesicle-associated membrane proteins.

Tajika Y, Takahashi M, Khairani AF, Ueno H, Murakami T, Yorifuji H.Author information Department of Anatomy, Gunma University Graduate School of Medicine, 3-39-22 Showa-machi, Maebashi, Gunma, 371-8511, Japan, ytajika@gunma-u.ac.jp.AbstractMyofibers have characteristic membrane compartments in their cytoplasm and sarcolemma, such as the sarcoplasmic reticulum, T-tubules, neuromuscular junction, and myotendinous junction. Little is known about the vesicular transport that is believed to mediate the development of these membrane compartments. We determined the locations of organelles in differentiating myotubes. Electron microscopic observation of a whole myotube revealed the arrangement of Golgi apparatus, rough endoplasmic reticulum, autolysosomes, mitochondria, and smooth endoplasmic reticulum from the perinuclear region toward the end of myotubes and the existence of a large number of vesicles near the ends of myotubes. Vesicles in myotubes were further characterized using immunofluorescence microscopy to analyze expression and localization of vesicle-associated membrane proteins (VAMPs). VAMPs are a family of seven proteins that regulate post-Golgi vesicular transport via the fusion of vesicles to the target membranes. Myotubes express five VAMPs in total. Vesicles with VAMP2, VAMP3, or VAMP5 were found near the ends of the myotubes. Some of these vesicles are also positive for caveolin-3, suggesting their participation in the development of T-tubules. Our morphological analyses revealed the characteristic arrangement of organelles in myotubes and the existence of transport vesicles near the ends of the myotubes.
Histochemistry and cell biology.Histochem Cell Biol.2013 Nov 22. [Epub ahead of print]
Myofibers have characteristic membrane compartments in their cytoplasm and sarcolemma, such as the sarcoplasmic reticulum, T-tubules, neuromuscular junction, and myotendinous junction. Little is known about the vesicular transport that is believed to mediate the development of these membrane compart
PMID 24263617

SNAP-23 and VAMP-3 contribute to the release of IL-6 and TNFα from a human synovial sarcoma cell line.

Boddul SV, Meng J, Dolly JO, Wang J.Author information International Centre for Neurotherapeutics, Dublin City University, Ireland.AbstractFibroblast-like synoviocytes are important mediators of inflammatory joint damage in arthritis through the release of cytokines, but it is unknown whether their exocytosis from these particular cells is SNARE-dependent. Here, the complement of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) in human synovial sarcoma cells (SW982) was examined with respect to the secretion of interleukin-6 (IL-6) and tumour necrosis factor α (TNFα), before and after knockdown of a synaptosome-associated protein of molecular mass 23 kDa (SNAP-23) or the vesicle-associated membrane protein 3 (VAMP-3). Wild-type SW982 cells expressed SNAP-23, VAMP-3, syntaxin isoforms 2-4 and synaptic vesicle protein 2C (SV2C). These cells showed Ca2+ -dependent secretion of IL-6 and TNFα when stimulated by interleukin-1β (IL-1β) or in combination with K+ depolarization. Specific knockdown of SNAP-23 or VAMP-3 decreased the exocytosis of IL-6 and TNFα; the reduced expression of SNAP-23 caused accumulation of SV2 in the peri-nuclear area. A monoclonal antibody specific for VAMP-3 precipitated SNAP-23 and syntaxin-2 (and syntaxin-3 to a lesser extent). The formation of SDS-resistant complexes by SNAP-23 and VAMP-3 was reduced upon knockdown of SNAP-23. Although the syntaxin isoforms 2, 3 and 4 are expressed in SW982 cells, knockdown of each did not affect the release of cytokines. Collectively, these results show that SNAP-23 and VAMP-3 participate in IL-1β-induced Ca2+ -dependent release of IL-6 and TNFα from SW982 cells.
The FEBS journal.FEBS J.2013 Nov 20. doi: 10.1111/febs.12620. [Epub ahead of print]
Fibroblast-like synoviocytes are important mediators of inflammatory joint damage in arthritis through the release of cytokines, but it is unknown whether their exocytosis from these particular cells is SNARE-dependent. Here, the complement of soluble N-ethylmaleimide-sensitive factor attachment pro
PMID 24373201

Related Pictures

Ver detalles de PROCESADOR BEHRINGER VAMP3 Convergência musical: Behringer inova com Behringer Vamp3 gitarren preamp Vamp3 by Drawloverlala on DeviantArt Vamp3 by theragnboneemporium on DeviantArt Behringer VAMP3 | Rapid Online vamp3 pedaleira multiefeitos behringer

★リンクテーブル★

リンク元	「小胞結合膜タンパク質3」「synaptobrevin 3」「vesicle-associated membrane protein 3」

「小胞結合膜タンパク質3」

Vesicle-associated membrane protein 3
	; PDB rendering based on 1kil.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1kil, 1n7s
Identifiers
Symbols	VAMP3; CEB
External IDs	OMIM: 603657 MGI: 1321389 HomoloGene: 3511 GeneCards: VAMP3 Gene
Gene Ontology
Molecular function	• protein binding; • syntaxin-1 binding;
Cellular component	• plasma membrane; • integral to membrane; • apical plasma membrane; • cell junction; • clathrin-coated vesicle; • secretory granule; • clathrin-coated vesicle membrane; • SNARE complex; • neuron projection; • synapse; • recycling endosome;
Biological process	• positive regulation of receptor recycling; • protein complex assembly; • exocytosis; • vesicle docking involved in exocytosis; • cellular membrane fusion; • vesicle-mediated transport; • calcium ion-dependent exocytosis; • substrate adhesion-dependent cell spreading; • retrograde transport, endosome to Golgi; • Golgi to plasma membrane protein transport;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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