Ask about this productRelated genes to: GNAI3 antibody
- Gene:
- GNAI3 NIH gene
- Name:
- G protein subunit alpha i3
- Previous symbol:
- -
- Synonyms:
- 87U6
- Chromosome:
- 1p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2018-03-05
Related products to: GNAI3 antibody
Related articles to: GNAI3 antibody
- Mesothelin (MSLN) is a glycosylphosphatidylinositol-anchored cell surface protein that is overexpressed in several solid tumors and in one-third of pediatric acute myeloid leukemia (AML) cases. It represents a validated immunotherapeutic target owing to its lack of expression in normal bone marrow. The function of MSLN in AML is unknown, but it is implicated to regulate adhesion in solid tumors through interaction with its only known binding partner, MUC16/CA125. This study uses CRISPR/Cas9 mutagenesis to generate knockout (KO) of MSLN in NOMO-1 and a MSLN-expressing patient-derived xenograft model to investigate its biological role in AML. We show that MSLN-KO cells proliferate slower, have reduced mitochondrial metabolism, are arrested in G1 cell cycle phase, adhere less to extracellular matrix in vitro and engraft slower in vivo. MSLN-KO cells also exhibit increased sensitivity to Ara-C and reduced extracellular matrix-mediated chemoprotection. Using an unbiased approach, we identify Src-family kinase member LYN, and guanine nucleotide-binding protein G(i) alpha subunit proteins, GNAI1, GNAI2, and GNAI3 as novel binding partners of MSLN in AML and show that pharmacological or genetic inhibition of LYN signaling restores NOMO-1 cell sensitivity to Ara-C. Together, these findings demonstrate that MSLN functions as an oncogenic driver in AML and reveal a previously unrecognized MSLN-LYN signaling axis, the therapeutic targeting of which may enhance responses to chemotherapy. - Source: PubMed
Publication date: 2026/03/20
Faust Joshua RHamill DarcyKolb E AndersStevens Alexandra MGopalakrishnapillai AnilkumarBarwe Sonali P - Osteoporosis, characterized by progressive bone loss and increased fracture risk, is a growing concern as the population ages. Current treatments, though advanced, remain limited, underscoring the necessity for novel therapeutic targets. Recent studies have shown that the immune system plays a key role in osteoporosis, with osteoclasts driving bone resorption. Gαi proteins, critical mediators of immune signaling, are implicated in osteoclastogenesis, but their precise role remains unclear. It is demonstrated that Gαi1/3 was highly expressed in osteoclast precursors and mature osteoclasts, with elevated levels in the bone marrow of osteoporotic patients and ovariectomized (OVX) mice. Conditional knockout of Gαi1/3 in osteoclast precursors mitigates OVX-induced bone loss, improving bone mass and structure. Gαi1/3-deficient bone marrow monocytes and macrophages exhibit impaired osteoclast formation and reduced bone resorption. In contrast, overexpression of Gαi1/3 enhances osteoclast differentiation and function. In addition, the 173 Asp residue of Gαi3 is identified as crucial for RANK-TRAF6 binding during RANKL signaling. Inhibition of Gαi1/3 mimics the protective effects of denosumab, a treatment for osteoporosis, in mice. The findings position Gαi1/3 as a critical regulator of osteoclastogenesis and suggest it as a promising therapeutic target for osteoporosis. - Source: PubMed
Publication date: 2026/02/12
Bai ChaowenZhang MingchaoLiu LeTao LideXu ChenyangChai HaoShi XinWang YinZhang XiaopeiChen QiongLiu DongBai JinyuShe ChangZhou XiaozhongCao CongShan Huajian - The aim of this study was to investigate the mechanism of action of SB on TRP-induced abnormalities of bone metabolism in LNCaP cells. - Source: PubMed
Publication date: 2026/01/29
Li JianhuiLv XuejiaoJiang Ying - Neuroblastoma RAS viral oncogene homolog (NRAS) mutations occur in 20-30% of cutaneous melanomas, defining a distinct molecular subtype. While NRAS mutations drive unique gene expression programs, locus-specific transcriptional regulation has not been systematically explored. This study characterized coordinated transcriptional upregulation in NRAS-mutant melanoma, focusing on chromosome 1p13.2. RNA-seq and mutation data for 472 melanoma samples from The Cancer Genome Atlas Skin Cutaneous Melanoma were analyzed. Differential expression, coexpression assessment, and copy number variation (CNV) correlation were performed for 45 protein-coding genes within 1p13.2. Findings were validated in MSK-IMPACT 2021 ( n = 696). In NRAS-mutant melanomas, 56% of 1p13.2 genes were upregulated (false discovery rate < 0.05) versus 12% genome-wide ( P < 0.001), including TRIM33, AMPD1, GNAI3, and SLC25A24. Upregulation was NRAS-specific: 84% showed higher expression versus BRAF-mutant tumors. Six of the 10 most NRAS-correlated genes localized to 1p13.2. CNV gains showed dose-dependent effects (gains: 1.8-3.2 fold; amplifications: 3.5-5.4 fold), with strong correlations (AMPD1 ρ = 0.68, GNAI3 ρ = 0.62, TRIM33 ρ = 0.58; P < 0.001). MSK-IMPACT validation confirmed 1p13.2 upregulation. As these findings are based on transcriptomic and copy number analyses, additional protein-level and functional studies across independent cohorts are required to confirm biological significance. NRAS-mutant melanomas harbor a coordinated transcriptional program within 1p13.2, driven by CNV gains. This locus contains genes with potential druggability, offering new avenues for combinatorial targeting alongside mitogen-activated protein kinase pathway inhibition. - Source: PubMed
Publication date: 2026/01/29
Bilik Sophie MBurke Olivia MElman Scott A - Prostate cancer (PCa) is the most prevalent malignancy among men worldwide. Advanced prostate cancer is characterized by aggressive progression, limited therapeutic response, and poor prognosis. Elucidating its oncogenic mechanisms may provide new opportunities for targeted intervention. Increasing evidence suggests that modulating cytoprotective autophagy represents a promising strategy for improving cancer treatment efficacy and overcoming drug resistance. Here, we identified the G protein subunit GNG4 as a crucial regulator of prostate cancer development. GNG4 expression was markedly elevated in advanced prostate cancer phenotypes and positively correlated with tumor survival, apoptosis, and migration. Further analysis demonstrated that GNG4 depletion suppressed autophagy and enhanced cellular sensitivity to enzalutamide. Mechanistically, GNG4 interacts with GNB1 to stabilize the downstream effector protein GNAI3 through the ubiquitination-proteasome pathway. These three distinct G protein subunits form a functional complex that regulates intracellular autophagy and subsequently influences the malignant behavior of prostate cancer. Furthermore, inhibition of autophagy or GNG4 knockdown significantly increased the antitumor efficacy of enzalutamide both in vitro and in vivo. Our findings identified GNG4 as a pivotal modulator of prostate cancer progression and proposed it as a promising therapeutic target to enhance the clinical response to enzalutamide. GNG4 interacts with GNB1 to stabilize GNAI3 via the ubiquitination-proteasome pathway, thereby activating autophagy. This process promotes prostate cancer progression and resistance to androgen receptor signaling inhibitors (ARSis). In contrast, GNG4 knockdown or pharmacological inhibition of autophagy restores ARSI sensitivity and suppresses tumor growth. - Source: PubMed
Publication date: 2026/01/28
Chen LeiZhang JingyanHu YanshuoPeng XufengWang HongChen BinghuaXia JunXue WeiPan Chun-Wu