VAMP1

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

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UniProt| |

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RefSeq (mRNA)| |

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Wikidata
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Vesicle-associated membrane protein 1 is a protein that in humans is encoded by the VAMP1 gene.[1][2]

## Contents

* 1 Function
* 2 Clinical significance
* 3 Interactive pathway map
* 4 References
* 5 Further reading

## Function

[edit | edit source]

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP1 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Multiple alternative splice variants that encode proteins with alternative carboxy ends have been described, but the full-length nature of some variants has not been defined.[2]

## Clinical significance

[edit | edit source]

Homozygous mutations in VAMP1 have been identified in a series of children affected with a form of congenital myasthenic syndrome and similar presynaptic features in these patients and the knock-out VAMP1 mouse have been demonstrated.[3]

## Interactive pathway map

[edit | edit source]

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

[[File:

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<imagemap> Image:NicotineDopaminergic_WP1602.png

|{{{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".

## References

[edit | edit source]

1. ↑ Archer BT, Ozçelik T, Jahn R, Francke U, Südhof TC (October 1990). "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2". The Journal of Biological Chemistry. 265 (28): 17267–73. PMID 1976629.
2. ↑ 2.0 2.1 "Entrez Gene: VAMP1 vesicle-associated membrane protein 1 (synaptobrevin 1)".
3. ↑ Salpietro V, Lin W, Delle Vedove A, Storbeck M, Liu Y, Efthymiou S, Manole A, Wiethoff S, Ye Q, Saggar A, McElreavey K, Krishnakumar SS, Pitt M, Bello OD, Rothman JE, Basel-Vanagaite L, Hubshman MW, Aharoni S, Manzur AY, Wirth B, Houlden H (April 2017). "Homozygous mutations in VAMP1 cause a presynaptic congenital myasthenic syndrome". Annals of Neurology. 81 (4): 597–603. doi:10.1002/ana.24905. PMC 5413866. PMID 28253535.

## Further reading

[edit | edit source]

* 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.
* Jagadish MN, Fernandez CS, Hewish DR, Macaulay SL, Gough KH, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel MJ, Ward CW (August 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". The Biochemical Journal. 317. 317 ( Pt 3): 945–54. doi:10.1042/bj3170945. PMC 1217577. PMID 8760387.
* 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.
* Weir ML, Klip A, Trimble WS (July 1998). "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP". The Biochemical Journal. 333. 333 ( Pt 2): 247–51. doi:10.1042/bj3330247. PMC 1219579. PMID 9657962.
* Isenmann S, Khew-Goodall Y, Gamble J, Vadas M, Wattenberg BW (July 1998). "A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal". Molecular Biology of the Cell. 9 (7): 1649–60. doi:10.1091/mbc.9.7.1649. PMC 25402. PMID 9658161.
* Nishimura Y, Hayashi M, Inada H, Tanaka T (January 1999). "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins". Biochemical and Biophysical Research Communications. 254 (1): 21–6. doi:10.1006/bbrc.1998.9876. PMID 9920726.
* Berglund L, Hoffmann HJ, Dahl R, Petersen TE (November 1999). "VAMP-1 has a highly variable C-terminus generated by alternative splicing". Biochemical and Biophysical Research Communications. 264 (3): 777–80. doi:10.1006/bbrc.1999.1588. PMID 10544008.
* 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.
* Imabayashi H, Mori T, Gojo S, Kiyono T, Sugiyama T, Irie R, Isogai T, Hata J, Toyama Y, Umezawa A (August 2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Experimental Cell Research. 288 (1): 35–50. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157.
* 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.

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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

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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

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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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