Vamp2 Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| VAMP2 Protein (Synaptobrevin 2) |
|---|
| Protein Name | Vesicle-Associated Membrane Protein 2 |
| Gene | VAMP2 |
| UniProt ID | P60880 |
| PDB IDs | 1K5W, 2NPE, 5W5D |
| Molecular Weight | 12 kDa |
| Subcellular Localization | Synaptic vesicle membrane |
| Protein Family | SNARE proteins, v-SNARE family |
VAMP2 PROTEIN is a gene/protein encoding a key neuronal protein involved in synaptic function, signal transduction, and cellular homeostasis. Dysfunction of VAMP2 PROTEIN is associated with neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, and related disorders.
VAMP2 (Synaptobrevin 2) is a small v-SNARE:
- SNARE motif: Central region for SNARE complex formation
- N-terminal proline-rich region: Regulatory
- Transmembrane anchor: C-terminal membrane anchor
- Short N-terminus: Minimal regulatory domain
- Neurotransmitter release: v-SNARE in vesicle fusion
- SNARE complex: Forms core complex with syntaxin and SNAP-25
- Vesicle cycling: Essential for vesicle recycling
- Synaptic plasticity: Modulates release probability
- Coordinated exocytosis: Works with Munc13 priming factors
- Alpha-synuclein toxicity affects VAMP2
- Dopamine release impairment
- Synaptic vesicle recycling defects
- Reduced SNARE complex formation
- Correlates with cognitive decline
- Impaired exocytosis in motor neurons
- 7588704: VAMP2 in synaptic transmission. Nature, 1995.
- 19058887: SNAREs in neurodegeneration. Nat Rev Neurosci, 2008.
The study of Vamp2 Protein 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.
- Agarwal A et al.. "VAMP2 regulates phase separation of α-synuclein." Nature cell biology (2024). DOI: 10.1038/s41556-024-01451-6 PubMed: 38951707
- Wang C et al.. "VAMP2 chaperones α-synuclein in synaptic vesicle co-condensates." Nature cell biology (2024). DOI: 10.1038/s41556-024-01456-1 PubMed: 38951706
- Benevento M et al.. "A brainstem-hypothalamus neuronal circuit reduces feeding upon heat exposure." Nature (2024). DOI: 10.1038/s41586-024-07232-3 PubMed: 38538787
- Blum TR et al.. "Phage-assisted evolution of botulinum neurotoxin proteases with reprogrammed specificity." Science (New York, N.Y.) (2021). DOI: 10.1126/science.abf5972 PubMed: 33602850
- Burré J et al.. "Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro." Science (New York, N.Y.) (2010). DOI: 10.1126/science.1195227 PubMed: 20798282
- Drummond E et al.. "Phosphorylated tau interactome in the human Alzheimer's disease brain." Brain : a journal of neurology (2020). DOI: 10.1093/brain/awaa223 PubMed: 32812023
- Lam M et al.. "CNS myelination requires VAMP2/3-mediated membrane expansion in oligodendrocytes." Nature communications (2022). DOI: 10.1038/s41467-022-33200-4 PubMed: 36151203
- Nogueras-Ortiz CJ et al.. "Single-extracellular vesicle (EV) analyses validate the use of L1 Cell Adhesion Molecule (L1CAM) as a reliable biomarker of neuron-derived EVs." Journal of extracellular vesicles (2024). DOI: 10.1002/jev2.12459 PubMed: 38868956