Ask about this productRelated genes to: G3BP1 antibody
- Gene:
- G3BP1 NIH gene
- Name:
- G3BP stress granule assembly factor 1
- Previous symbol:
- -
- Synonyms:
- HDH-VIII, G3BP
- Chromosome:
- 5q33.1
- Locus Type:
- gene with protein product
- Date approved:
- 2006-10-25
- Date modifiied:
- 2016-02-29
Related products to: G3BP1 antibody
Related articles to: G3BP1 antibody
- Alzheimer's disease (AD) is characterized by progressive neurodegeneration driven by amyloid-β (Aβ) plaques and tau neurofibrillary tangles. Stress granules (SGs), dynamic ribonucleoprotein condensates formed under cellular stress have been implicated in several neurodegenerative disorders, but their role in AD pathogenesis remains incompletely understood. - Source: PubMed
Publication date: 2026/05/31
Kashtiban Bita AshrafiRezazadeh MaryamGharesouran JalalJafari BehboudGhafouri-Fard Soudeh - Ras-GTPase activating protein SH3 domain-binding protein 1 (G3BP1), a core component of stress granules (SGs), is highly expressed in several liver diseases. SG assembly has also been observed in metabolic disorders, suggesting that this process may be a promising therapeutic target. Using a high-content drug screening approach based on G3BP1 expression, we identified Micranthin B (MB), a diterpenoid from Isodon lophanthoides (Buch.-Ham. ex D. Don) Hara, as a compound that alleviates metabolic dysfunction-associated steatohepatitis (MASH) by targeting G3BP1 and inhibiting SG formation. MB administration significantly alleviated MASH progression in both high-fat, high-cholesterol (HFHC) diet-induced mouse model and palmitic acid (PA)-stimulated hepatocytes. Mechanistically, MB inhibited histone deacetylase 6 (HDAC6)-mediated deacetylation of G3BP1, thereby suppressing SG formation. This prevented SG-mediated recruitment of the N-glycosylation-related proteins SEC61 translocon subunit beta (SEC61B) and calnexin (CANX), reduced the accumulation of misfolded or unfolded proteins, and alleviated endoplasmic reticulum (ER) stress. These findings suggest that MB has therapeutic potential in the treatment of MASH. - Source: PubMed
Cheng YangWang JingyiHe MengmengWu EnyiYe ShengtaoZheng YingZhang YanqiuKong LingyiZhang Hao - Ferroptosis is a key mechanism leading to neural damage in acute ischemic stroke (AIS). The production of stress granules (SGs) has also been reported to regulate AIS injury. However, the intrinsic link between SG formation and ferroptosis remains poorly understood. This investigation examined the interaction between the SG core protein G3BP1 and ferritin heavy chain 1 (FTH1) in AIS and its role in controlling ferroptosis. Using models of middle cerebral artery occlusion/reperfusion (MCAO/R) in rats and oxygen-glucose deprivation/reoxygenation (OGD/R) in cells, together with immunofluorescence, co-immunoprecipitation (Co-IP), and the detection of ferroptosis, we observed that SG formation was inversely correlated with ferroptotic injury during AIS. G3BP1 and FTH1 interact dynamically during AIS injury, and the extent of this interaction was positively correlated with FTH1 protein level and inversely with the severity of ferroptosis. Functional experiments further demonstrated that the deficiency of G3BP1 inhibits the formation of stress granules (SGs), exacerbates the down - regulation of FTH1, and enhances ferroptosis. In contrast, the overexpression of G3BP1 promotes the assembly of SGs, maintains the expression of FTH1, and consequently mitigates ferroptotic injury. The results of this study indicate that G3BP1 and stress granule formation are closely correlated with the maintenance of FTH1 protein levels, thereby mitigating ferroptotic damage in acute ischemic stroke (AIS). This finding provides new experimental evidence supporting a protective role for SG in ferroptosis, thereby presenting an innovative perspective and a potential therapeutic target for AIS. - Source: PubMed
Publication date: 2026/05/28
Sun BinRuan ZiyunYou RuijiaLuo JingSi Wenwen - Biomolecular condensates are a major driver of cellular organization; however, we lack a predictable and systematic approach to modulate the multivalent interactions underlying their formation. Here, we demonstrate that the AI-driven FragFold method enables robust and generalizable design of protein fragments to control biomolecular condensate formation. We apply this approach across diverse proteins: G3BP1, SARS-CoV-2 nucleocapsid, TDP-43, and focal adhesion kinase (FAK). Computationally screening 2,235 fragments, we selected 18 candidates for further investigation. Overall, we attain a 50% success rate (9/18 designs) in discovering condensate-controlling protein fragments, experimentally testing just 3-5 candidates per protein. For each condensate-forming protein, the success rate is at least 40%. Furthermore, FragFold-predicted fragment binding modes align with their condensate-inhibitory or -enhancing activities, revealing both known and newly identified interactions underlying condensate formation. In FAK, a condensate-inhibitory fragment uncovered a domain interaction required for phase separation, and mutational analysis validated its importance. Notably, this inhibitory fragment also suppresses FAK condensate formation in living mammalian cells. Together, these results establish AI-guided protein fragment discovery as a generalizable strategy to dissect and control the molecular interactions that govern biomolecular condensates. - Source: PubMed
Publication date: 2026/05/12
Savinov AndrewSadasivan JibinWhite Kyle JRubien Jack DLi Gene-WeiCase Lindsay B - Antisense oligonucleotides (ASOs) enter cells efficiently, but the compartment from which productive escape occurs remains uncertain. We used live-cell microscopy, ratiometric pH measurements and 3D focused ion beam scanning electron microscopy (FIB-SEM) in U2OS cells to track a -targeting ASO from uptake to delivery. The ASO entered by endocytosis and accumulated in late endosomes, endolysosomes and lysosomes, where it induced luminal neutralization without galectin-3 recruitment or limiting-membrane rupture. Under conditions that reduced -RNA by >90%, quantitative imaging showed that less than 4% of internalized ASOs reached the nucleus. L-leucyl-L-leucine methyl ester (LLOMe)-induced membrane damage released co-internalized dextran but not ASOs, showing that ASOs remain sequestered even in damaged late endocytic compartments. In apilimod-expanded organelles, ASOs concentrated at limiting membranes and intraluminal foci with constrained motion, consistent with association with membrane and luminal structures. Although G3BP1/2 has been proposed to plug damaged endocytic membranes, we detected no recruitment of G3BP1 to endosomes or lysosomes; loss of G3BP1 and G3BP2 increased functional delivery modestly. We therefore propose that productive escape occurs earlier in endocytosis, most likely in early or recycling endosomes, where ASOs would still be unbound within the lumen and where membrane fusion and fission could generate perforations permitting release. - Source: PubMed
Publication date: 2026/05/13
Sitarska EwaSaminathan AnandScanavachi GustavoSomerville ElliottCourtney Margo FReid Dylan ADanielsen Mathias BogetoftDavidsen Fie Kristine NoergaardJensen Knud JBennett C FrankKirchhausen Tom