G3Bp1 is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| G3BP1 |
|---|
| Gene Symbol | G3BP1 |
| Full Name | Ras-GTPase-Activating Protein Binding Protein 1 |
| Chromosomal Location | 5q33.1 |
| NCBI Gene ID | 10193 |
| OMIM ID | - |
| Ensembl ID | ENSG00000130830 |
| UniProt ID | Q9UBZ9 |
| Associated Diseases | ALS, FTD, Alzheimer's Disease |
G3BP1 is a gene/protein encoding a key neuronal protein involved in synaptic function, signal transduction, and cellular homeostasis. Dysfunction of G3BP1 is associated with neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, and related disorders.
G3BP1 (Ras-GTPase-Activating Protein Binding Protein 1) is a 524-amino acid protein that functions as a major scaffold protein in stress granules. It plays critical roles in:
- Stress granule assembly: Central organizer of stress granule formation
- mRNA decay regulation: Interacts with decay enzymes
- Signal transduction: Links Ras signaling to stress responses
- Translation repression: Sequesters mRNAs during stress
- Neuroprotection: Regulates neuronal stress responses
- G3BP1 is a core component of stress granules
- Mutations in stress granule proteins (G3BP1, TIA1) linked to ALS
- Dysregulated stress granule dynamics contribute to motor neuron degeneration
- Interacts with other ALS proteins: TDP-43, FUS, C9orf72
- Stress granule pathology in FTD
- Overlapping molecular mechanisms with ALS
- RNA metabolism dysregulation
- Altered stress granule dynamics in AD
- Links between stress responses and amyloid pathology
G3BP1 is widely expressed in the brain:
- High expression in motor neurons
- Expressed in hippocampal neurons
- Present in cortical neurons
- Links to Allen Brain Atlas expression data
- 19179225: G3BP1 in stress granule formation. Mol Cell, 2009.
- 25468282: ALS mutations in stress granule proteins. Nat Neurosci, 2014.
- 33268865: Stress granules in neurodegeneration. Nat Rev Neurosci, 2020.
The study of G3Bp1 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
- Yao RQ et al.. "Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles." Autophagy (2021). DOI: 10.1080/15548627.2020.1725377 PubMed: 32048886
- Freibaum BD et al.. "Identification of small molecule inhibitors of G3BP-driven stress granule formation." The Journal of cell biology (2024). DOI: 10.1083/jcb.202308083 PubMed: 38284934
- Cui Q et al.. "Diverse CMT2 neuropathies are linked to aberrant G3BP interactions in stress granules." Cell (2023). DOI: 10.1016/j.cell.2022.12.046 PubMed: 36738734
- Glineburg MR et al.. "Stress granule formation helps to mitigate neurodegeneration." Nucleic acids research (2024). DOI: 10.1093/nar/gkae655 PubMed: 39106168
- 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
- Fang MY et al.. "Small-Molecule Modulation of TDP-43 Recruitment to Stress Granules Prevents Persistent TDP-43 Accumulation in ALS/FTD." Neuron (2019). DOI: 10.1016/j.neuron.2019.05.048 PubMed: 31272829