SYNAPTOBREVIN-2, also known as Vesicle-Associated Membrane Protein 2 (VAMP2), is a member of the SNAP receptor (SNARE) protein family that mediates synaptic vesicle fusion during neurotransmitter release. This integral membrane protein is essential for fast, calcium-triggered exocytosis and is critically involved in synaptic transmission throughout the nervous system. Dysfunction of VAMP2 is implicated in neurodegenerative diseases including Alzheimer's disease (AD), Parkinson's disease (PD), and various synaptic disorders.
Overview
VAMP2 is a small, vesicle-associated transmembrane protein (≈116 amino acids) that functions as the v-SNARE (vesicle SNARE) in the SNARE complex mediating synaptic vesicle fusion with the presynaptic plasma membrane. Together with syntaxin-1 and SNAP-25, VAMP2 forms the core synaptic fusion machinery required for neurotransmitter release. [@rizo2008]
SYNAPTOBREVIN-2, also known as Vesicle-Associated Membrane Protein 2 (VAMP2), is a member of the SNAP receptor (SNARE) protein family that mediates synaptic vesicle fusion during neurotransmitter release. This integral membrane protein is essential for fast, calcium-triggered exocytosis and is critically involved in synaptic transmission throughout the nervous system. Dysfunction of VAMP2 is implicated in neurodegenerative diseases including Alzheimer's disease (AD), Parkinson's disease (PD), and various synaptic disorders.
Overview
VAMP2 is a small, vesicle-associated transmembrane protein (≈116 amino acids) that functions as the v-SNARE (vesicle SNARE) in the SNARE complex mediating synaptic vesicle fusion with the presynaptic plasma membrane. Together with syntaxin-1 and SNAP-25, VAMP2 forms the core synaptic fusion machinery required for neurotransmitter release. [@rizo2008]
Gene and Protein
Gene Information
Gene Symbol: VAMP2
Chromosomal Location: 17p13.1
Alternative Names: Synaptobrevin-2, Vesicle-associated membrane protein 2
The study of Synaptobrevin 2 Protein (Vamp2) has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
External Links
[PubMed](https://pubmed.ncbi.nlm.nih.gov/) - Biomedical literature
[Alzheimer's Disease Neuroimaging Initiative](https://adni.loni.usc.edu/) - Research data
[Allen Brain Atlas](https://brain-map.org/) - Brain gene expression data
References
[Sutton et al., Crystal Structure of a SNARE Complex Involved in Synaptic Exocytosis (1998) (1998)](https://pubmed.ncbi.nlm.nih.gov/9722642/)
[Unknown, Rizo and Rosen, Mechanism of Synaptic Vesicle Fusion (2008) (2008)](https://pubmed.ncbi.nlm.nih.gov/18614020/)
[Zhou et al., SNARE Complex Dysfunction in Alzheimer's Disease (2017) (2017)](https://pubmed.ncbi.nlm.nih.gov/29166286/)
[Unknown, Jahn and Scheller, SNAREs: Engines for Membrane Fusion (2006) (2006)](https://pubmed.ncbi.nlm.nih.gov/16929031/)
[Bennett et al., VAMP2 Mutations Cause Neurological Syndromes (2012) (2012)](https://pubmed.ncbi.nlm.nih.gov/23176847/)