GRB2 _ ASH
- Known as:
- GRB2 _ ASH
- Catalog number:
- GTX22234
- Product Quantity:
- 100 µg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- GRB2 _ ASH
Related genes to: GRB2 _ ASH
- 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 _ ASH
Related articles to: GRB2 _ ASH
- Sorafenib resistance remains a major therapeutic challenge in advanced hepatocellular carcinoma (HCC). This study aimed to investigate the role of growth factor receptor-bound protein 2 (GRB2) in sorafenib resistance of HCC cells under hypoxic conditions and to elucidate the underlying molecular mechanisms involving the PI3K/AKT signaling pathway. - Source: PubMed
Publication date: 2026/05/06
He JiaqianKong YinzhiWang YunyongFang QiaolingWu HemengDu KeweiLuo YuzhenTan JinnaYin HuiLin HongshengLi Mingfen - Pregnancy-related breast cancer is relatively rare, but its incidence is increasing as the age of childbearing advances. The impact of placenta-specific microRNAs (miRNAs) derived from the chromosome 19 miRNA cluster (C19MC) on pregnancy-associated breast cancer is unclear. Nuclear protein high mobility group box 3 (HMGB3) plays a role in cancer progression. This study examined the effects of placenta-specific C19MC miRNAs on the cancer-related gene HMGB3 in the human breast cancer cell line MCF-7. - Source: PubMed
Sato AiTakei HiroyukiNoguchi SyunyaTakizawa Toshihiro - Lung adenocarcinoma (LUAD) is the main histologic subtype of lung cancer, and its incidence is on the rise. However, since the vast majority of patients are already in advanced stages at the time of diagnosis, their 5-year survival rate is only 15%, so it is urgent to explore the mechanism of the development of LUAD and improve the survival time of patients. Interleukin-11 (IL-11), a member of the IL-6 cytokine family, has an influential role in the development and progression of a variety of tumors, but the specific molecular mechanisms that promote the malignant progression of LUAD are unknown. Here, we found that the IL-11-induced activation of Akt, Erk, and STAT3 could be inhibited by knocking out the expression of Gαi1/3. In contrast, overexpression of Gαi1/3 could enhance IL-11-induced signaling. The binding of Gαi1/3 to GP130 mediates IL-11-induced downstream activation of Akt-mTOR, Erk, and STAT3, which requires recruitment of Grb2-associated binding protein 1 (Gab1). In LUAD cells, shGαi1/3 inhibited cell growth, proliferation, and migration as well as blocked the tumor-promoting ability of IL-11. However, overexpression of Gαi1/3 enhanced the IL-11-induced cell growth, proliferation, and migration. ShGαi1/3 also inhibited the proliferation of LUAD cells in vivo. Overall, the findings of this study demonstrate the Gαi1 and Gαi3 are critical for IL-11 signal transduction. Moreover, we reveal that Gαi1 and Gαi3 are highly expressed and associated with poor overall survival in lung adenocarcinoma and may thus act as potential therapeutic targets in LUAD. These results provide a novel therapeutic strategy for LUAD patients with upregulated IL-11 expression. - Source: PubMed
Publication date: 2026/04/25
Luo GaomengHu WenxuanYang JianLu ZhengCui YuanZeng WeibiaoDing HaoLi QifanChen ZhikeTong XinDing ChengXu ChunZhao Jun - Receptor tyrosine kinase signaling is initiated by extracellular ligand binding, which drives the formation of membrane-protein assemblies that activate intracellular signal transduction. Accurately resolving the molecular composition of these assemblies in situ remains challenging due to their nanoscale dimensions and intrinsic heterogeneity. Here, we introduce a single-molecule super-resolution imaging and analysis workflow designed to resolve and quantitatively characterize individual membrane-protein assembly sites in cells. We apply this approach to the nanoscale organization of the epidermal growth factor receptor (EGFR) and its adaptor protein Grb2 following stimulation with the native ligand epidermal growth factor. As activation progresses, we observe a reduction in EGFR density at the plasma membrane, a progressive accumulation of Grb2 at EGFR assembly sites, and an increase in both dimeric and higher-order oligomeric EGFR. The experimental and analytical framework presented here is broadly applicable to the study of diverse membrane-protein assemblies. - Source: PubMed
Kaminer AlexandraLi YunqingBarth Hans-DieterDietz Marina SHeilemann Mike - FCRL1 is a plasma membrane coreceptor on B cells that has been shown to potentiate B cell receptor (BCR)-driven calcium flux and negatively regulate ERK phosphorylation in a GRB2 and tyrosine-dependent manner. Of the proteins that associate with FCRL1, the recruitment of the inositol phosphatase SHIP-1 is GRB2 dependent, implicating SHIP-1 in FCRL1-mediated ERK regulation. Using immunoprecipitation and Western blotting, it was found that a proline-rich region in the C-terminus of SHIP-1, rather than its N-terminal SH2 domain, mediates recruitment of SHIP-1 to Y281 in FCRL1 in a manner dependent on GRB2. Interestingly, Y281 and GRB2 were also required for FCRL1 colocalization to the BCR. Translational fusions between tyrosine-mutated FCRL1 and the SH2 domain of SHIP-1 were sufficient to drive both colocalization of FCRL1 with the BCR as well as the ERK-inhibitory activity of FCRL1. Our data are consistent with a function for SHIP-1 as an adapter between FCRL1 and the BCR signalosome, and that this adapter function is responsible for BCR/FCRL1 colocalization after BCR stimulation and modulation of ERK signaling. - Source: PubMed
Wolfe Malory MTallon Arranz RutZenni Elizabeth LWilson Timothy J