GRB2 Pre-design Chimera RNAi
- Known as:
- GRB2 Pre-design Chimera RNAi
- Catalog number:
- H00002885-R02
- Product Quantity:
- 10 nmol
- Category:
- -
- Supplier:
- Abno
- Gene target:
- GRB2 Pre-design Chimera RNAi
Related genes to: GRB2 Pre-design Chimera RNAi
- Gene:
- GRB2 NIH gene
- Name:
- growth factor receptor bound protein 2
- Previous symbol:
- -
- Synonyms:
- NCKAP2
- Chromosome:
- 17q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-03-04
- Date modifiied:
- 2016-10-05
Related products to: GRB2 Pre-design Chimera RNAi
Related articles to: GRB2 Pre-design Chimera RNAi
- Oncogenic fusion proteins involving receptor tyrosine kinases can hijack cell signaling cascades to promote oncogenesis. Here, we show that the TRK-T3 fusion protein, generated by joining the N-terminal region of the condensate-forming protein TFG with the C-terminal region of TrkA, assembles into sheet-like biomolecular condensates after putative prewetting of the ER. These structures are distinct from those formed by either parent protein. We find that ER wetting and the condensate morphology of TRK-T3 are controlled by a hydrophobic transmembrane segment encoded in the TrkA moiety. Removing this segment abolishes the sheet-like morphology of TRK-T3 condensates in cells and in vitro. This loss of morphology diminishes the recruitment of the first-layer signal-transduction protein GRB2 and suppresses activation of the MAPK pathway. A minimal segment that mimics the transmembrane domain efficiently disrupts TRK-T3 condensation. Together, our findings highlight condensate morphology as an encoded property of this oncogenic fusion protein, controlling the alignment and signaling competence of TRK-T3 assemblies. They further suggest that hydrophobic interactions within TRK-T3 condensates represent a potential vulnerability in this oncogenic signaling mechanism. - Source: PubMed
Publication date: 2026/06/17
Chavez Sindy RBogus Savannah MCheung Samantha NZhou WinnieGudmundsson LiljaKato KahoErnst Andreas M - Microalgal protein (MP, Spirulina) is a highly promising novel sustainable protein resource, yet the mechanisms by which it regulates the production performance and milk quality of lactating dairy cows remain unclear. This study elucidates the regulatory mechanisms by which amino acid balancing and MP supplementation modulate production performance and milk quality in mid-lactation dairy cows fed low-protein diet (LPD). Results demonstrated that dietary interventions significantly altered milk composition. To elucidate the underlying molecular mechanisms, proteomic and metabolomic analyses were employed, leading to the identification of 1186 differentially expressed proteins (DEPs) and 1167 differentially expressed metabolites (DEMs). Key signaling molecules, such as GNB1, GNG5, GNG10, and GRB2, interacted with metabolic hubs like α-ketoglutaric acid/Glutamic acid within a regulatory network, enhancing amino acid sensing and signal transduction. The observed coordinated changes in key signaling molecules and metabolic hubs suggest that amino acid sensing and signal transduction pathways may be activated, potentially promoting energy metabolism and nitrogen conversion efficiency. The identified key molecular markers of milk quality lay a scientific basis for the production of high-quality dairy raw materials and the development of value-added dairy products. - Source: PubMed
Publication date: 2026/06/16
He TianleRen WenyiYang ShuangmingBai JinniGuo YajunWu YongjiangShi JinpingYue Caijuan - Atherosclerosis is a major cause of ischemic stroke and is characterized by complex immune-metabolic dysregulation. VAV3, a Rho guanine nucleotide exchange factor, regulates multiple cellular processes, but its role in vascular pathology remains unclear. This study aimed to explore the function and mechanism of VAV3 in atherosclerosis. - Source: PubMed
Publication date: 2026/06/04
Wang GuorongPu ChenLi QingLiu QiangWan XiaobinDeng JunDai MinXie BinHuang LianghuiZhao YanPing - Dynamic protein complex assembly is critical for regulating various biological processes. Proximity labeling (PL), best represented by the ascorbate peroxidase APEX2, allows these molecular events to be captured in living cells in a spatiotemporal manner. However, the hydrogen peroxide (HO) dependence of APEX2 has hindered its application in sensitive living systems. Here we introduce ROProx, a radical- and oxygen-driven photoreactive PL technology that leverages the chemically evolved biotin-naphthylamine probe BN2, which has strong binding affinity for APEX2, and the unexpected tyrosyl radicals in APEX2. ROProx labels dynamic cytosolic protein complexes in living cells within seconds, with a range of 10 nm, and is precisely controlled by mild blue light irradiation without HO. Additionally, we apply ROProx to explore the phosphotyrosine-dependent GRB2 interactome in living mice by simply injecting BN2 for 5 minutes. ROProx should, therefore, open broad opportunities for PL chemical evolution and applications in other living systems. - Source: PubMed
Publication date: 2026/05/28
Ke MiLiang FuchaoWang GuangqinHe AnMa BaixuLiu ZheyiWang JieXu YanLi YanliDong ZheZhong ZhihuaTang ZhiyaoSun PengyuHe KangminWang FangjunLiu ZhiyongYang XuemingTao LizhiTian Ruijun - - Source: PubMed
Publication date: 2026/05/28
Wittayavimol NattamolphanIwabuchi ErinaSasano HironobuSwart Amanda CBoonyaratanakornkit Viroj