VAMP3

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Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

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RefSeq (mRNA)| |

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

## Contents

* 1 Function
* 2 Interactions
* 3 References
* 4 Further reading

## Function

[edit | edit source]

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 | edit source]

VAMP3 has been shown to interact with

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

## References

[edit | edit source]

1. ↑ Bernstein AM, Whiteheart SW (January 1999). "Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets". Blood. 93 (2): 571–9. PMID 9885218.
2. ↑ 2.0 2.1 "Entrez Gene: VAMP3 vesicle-associated membrane protein 3 (cellubrevin)".
3. ↑ Annaert WG, Becker B, Kistner U, Reth M, Jahn R (December 1997). "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31". The Journal of Cell Biology. 139 (6): 1397–410. doi:10.1083/jcb.139.6.1397. PMC 2132629. PMID 9396746.
4. ↑ Hager HA, Roberts RJ, Cross EE, Proux-Gillardeaux V, Bader DM (February 2010). "Identification of a novel Bves function: regulation of vesicular transport". The EMBO Journal. 29 (3): 532–45. doi:10.1038/emboj.2009.379. PMC 2830705. PMID 20057356.
5. ↑ 5.0 5.1 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.
6. ↑ 6.0 6.1 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". Journal of Immunology. 164 (11): 5850–7. doi:10.4049/jimmunol.164.11.5850. PMID 10820264.
7. ↑ Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ (April 2003). "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain". The Journal of Biological Chemistry. 278 (15): 13462–7. doi:10.1074/jbc.M210483200. PMID 12556468.
8. ↑ 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
9. ↑ 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.
10. ↑ 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". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.

## Further reading

[edit | edit source]

* Timmers KI, Clark AE, Omatsu-Kanbe M, Whiteheart SW, Bennett MK, Holman GD, Cushman SW (December 1996). "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein". The Biochemical Journal. 320. 320 ( Pt 2) (2): 429–36. doi:10.1042/bj3200429. PMC 1217948. PMID 8973549.
* Annaert WG, Becker B, Kistner U, Reth M, Jahn R (December 1997). "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31". The Journal of Cell Biology. 139 (6): 1397–410. doi:10.1083/jcb.139.6.1397. PMC 2132629. PMID 9396746.
* Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, Niemann H, Louvard D (June 1998). "A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells". Molecular Biology of the Cell. 9 (6): 1437–48. doi:10.1091/mbc.9.6.1437. PMC 25366. PMID 9614185.
* Riento K, Galli T, Jansson S, Ehnholm C, Lehtonen E, Olkkonen VM (September 1998). "Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells". Journal of Cell Science. 111. 111 ( Pt 17): 2681–8. PMID 9701566.
* Prekeris R, Klumperman J, Chen YA, Scheller RH (November 1998). "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes". The Journal of Cell Biology. 143 (4): 957–71. doi:10.1083/jcb.143.4.957. PMC 2132958. PMID 9817754.
* 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". Journal of Immunology. 164 (11): 5850–7. doi:10.4049/jimmunol.164.11.5850. PMID 10820264.
* Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard GF, Jahn R (December 2000). "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". The EMBO Journal. 19 (23): 6453–64. doi:10.1093/emboj/19.23.6453. PMC 305878. PMID 11101518.
* Wade N, Bryant NJ, Connolly LM, Simpson RJ, Luzio JP, Piper RC, James DE (June 2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells". The Journal of Biological Chemistry. 276 (23): 19820–7. doi:10.1074/jbc.M010838200. PMID 11278762.
* Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR (February 2002). "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs". Nature Structural Biology. 9 (2): 107–11. doi:10.1038/nsb746. PMID 11786915.
* Poschet JF, Skidmore J, Boucher JC, Firoved AM, Van Dyke RW, Deretic V (April 2002). "Hyperacidification of cellubrevin endocytic compartments and defective endosomal recycling in cystic fibrosis respiratory epithelial cells". The Journal of Biological Chemistry. 277 (16): 13959–65. doi:10.1074/jbc.M105441200. PMID 11809765.
* 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". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.
* 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.
* Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
* 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.
* Dai J, Li J, Bos E, Porcionatto M, Premont RT, Bourgoin S, Peters PJ, Hsu VW (November 2004). "ACAP1 promotes endocytic recycling by recognizing recycling sorting signals". Developmental Cell. 7 (5): 771–6. doi:10.1016/j.devcel.2004.10.002. PMID 15525538.
* Boal F, Zhang H, Tessier C, Scotti P, Lang J (December 2004). "The variable C-terminus of cysteine string proteins modulates exocytosis and protein-protein interactions". Biochemistry. 43 (51): 16212–23. doi:10.1021/bi048612+. PMID 15610015.
* 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.

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PDB gallery

* 1kil: Three-dimensional structure of the complexin/SNARE complex

1kil: Three-dimensional structure of the complexin/SNARE complex

* 1n7s: High Resolution Structure of a Truncated Neuronal SNARE Complex

1n7s: High Resolution Structure of a Truncated Neuronal SNARE Complex

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Membrane protein: vesicular transport proteins (TC 1F)

Synaptic vesicle|

| SNARE|

| Q-SNARE|

* 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

|

R-SNARE|

* Synaptobrevin/VAMP: VAMP1
* VAMP2
* VAMP3

Synaptotagmin|

* SYT1
* SYT2
* SYT3
* SYT4
* SYT5
* SYT6
* SYT7
* SYT8
* SYT9
* SYT10
* SYT11
* SYT12
* SYT13
* SYT14
* SYT15
* SYT16
* SYT17

Other|

* Synaptophysin
* Synapsin

* Small GTPase: RAB3A

COPI|

* Coatomer
* COPA
* COPB1
* COPB2
* COPD/Archain
* COPE
* COPG
* COPG2
* COPZ1
* COPZ2

* Small GTPase: ARF

COPII|

* Coatomer
* SEC23A/SEC24A
* SEC13/SEC31

* Small GTPase: SAR1A

RME/Clathrin|

* CLTA
* CLTB
* CLTC

Caveolae|

* Caveolin (CAV1
* CAV2
* CAV3)

Other/ungrouped|

| Vesicle formation|

| 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

Small GTPase|

* Dynamin
* DNM1
* DNM2
* DNM3

Other|

* EHD protein family: EHD1
* EHD2
* EHD3
* EHD4

* Sorting nexins

* Vacuolar protein sorting: VPS13B
* VPS33B

* SYNRG

See also vesicular transport protein disorders

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