G3Bp2 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.
| G3BP2 Protein |
| Protein Name | Ras-GTPase-Activating Protein Binding Protein 2 |
| Gene | G3BP2 |
| UniProt ID | Q9UQF2 |
| PDB IDs | 3DIS, 4FCG |
| Molecular Weight | 52 kDa |
| Subcellular Localization | Cytoplasm, stress granules |
| Protein Family | G3BP family |
G3BP2 PROTEIN is a gene/protein encoding a key neuronal protein involved in synaptic function, signal transduction, and cellular homeostasis. Dysfunction of G3BP2 PROTEIN is associated with neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, and related disorders.
G3BP2 is a paralog of G3BP1 with similar domain organization:
- NTF2-like domain: Central dimerization domain
- RRM domain: RNA recognition
- RG-rich region: Low-complexity prion-like domain
- Stress granule assembly: Co-organizes with G3BP1
- mRNA regulation: Participates in mRNA storage
- Signal integration: Stress response signaling
- Compensatory roles: Redundant with G3BP1
- Compensates for G3BP1 dysfunction
- Stress granule abnormalities in ALS
- Similar stress granule involvement
- 19179225: G3BP proteins in stress granules. Mol Cell, 2009.
- 31748259: G3BP2 function. Autophagy, 2020.
The study of G3Bp2 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.
- Prentzell MT et al.. "G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling." Cell (2021). DOI: 10.1016/j.cell.2020.12.024 PubMed: 33497611
- Ru S et al.. "Human DBR1 deficiency impairs stress granule-dependent PKR antiviral immunity." The Journal of experimental medicine (2025). DOI: 10.1084/jem.20240010 PubMed: 39636299
- Jia X et al.. "De novo variants in genes regulating stress granule assembly associate with neurodevelopmental disorders." Science advances (2022). DOI: 10.1126/sciadv.abo7112 PubMed: 35977029
- Wang C et al.. "Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation." Neuron (2023). DOI: 10.1016/j.neuron.2023.05.033 PubMed: 37385246
- Sahoo PK et al.. "Disruption of G3BP1 granules promotes mammalian CNS and PNS axon regeneration." Proc Natl Acad Sci U S A (2025). DOI: 10.1073/pnas.2411811122 PubMed: 40014573
- Liau WS et al.. "Fear extinction is regulated by the activity of long noncoding RNAs at the synapse." Nature communications (2023). DOI: 10.1038/s41467-023-43535-1 PubMed: 37993455
- Li T et al.. "Downregulation of G3BP2 reduces atherosclerotic lesions in ApoE-/- mice." Atherosclerosis (2020). DOI: 10.1016/j.atherosclerosis.2020.08.003 PubMed: 32919187
- Sato K, Takayama KI, Inoue S. "Stress granules sequester Alzheimer's disease-associated gene transcripts and regulate disease-related neuronal proteostasis." Aging (2023). DOI: 10.18632/aging.204737 PubMed: 37219408