Ask about this productRelated genes to: Shc1 antibody
- Gene:
- SHC1 NIH gene
- Name:
- SHC adaptor protein 1
- Previous symbol:
- SHC
- Synonyms:
- p66, ShcA
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-02-17
- Date modifiied:
- 2016-10-05
Related products to: Shc1 antibody
Related articles to: Shc1 antibody
- Diabetic kidney disease (DKD) represents one of the most severe complications of diabetes. Although EZH2 (Enhancer of Zeste Homolog 2) has been implicated in renal injury and diabetes, its specific function within renal tubular cells in DKD remains unclear. Here, we explored the role and downstream mechanism of tubular EZH2 in DKD progression. Renal EZH2 expression was significantly upregulated in DKD. Single-nucleus RNA sequencing and immunofluorescence analyses verified that such elevation was restricted to proximal tubular epithelial cells. Conversely, tubular-specific deletion of Ezh2 exacerbated renal dysfunction and fibrosis in DKD mice. In vitro gain- and loss-of-function experiments in high glucose-stimulated HK2 cells further validated that EZH2 plays a renoprotective role under diabetic conditions. Mechanistically, we demonstrated that EZH2 epigenetically suppresses the pro-oxidative mediator SHC1. In the DKD mouse model, renal SHC1 protein abundance was markedly increased upon tubular Ezh2 knockout, accompanied by reduced levels of antioxidant enzymes SOD1 and SOD2, significantly elevated MDA, and depleted GSH. Consistent with these in vivo observations, in vitro functional assays further validated that EZH2 epigenetically downregulates SHC1 and alleviates such oxidative stress perturbations. Finally, we verified that SHC1 inhibition rescues the exacerbated fibrotic response and oxidative damage triggered by pharmacological EZH2 suppression under high-glucose conditions. In conclusion, tubular EZH2 protects against DKD via inhibiting SHC1-driven oxidative stress. - Source: PubMed
Publication date: 2026/08/10
Xu QimingLin PinglanChen SijunLu JianraoLi LinMoghadasali RezaYang XuejunHu JingWu MingChen Dongping - Beyond established rare fusions, such as ALK and ROS1, emerging ultrarare fusions involving receptor tyrosine kinases or their ligands, including EGFR-SHC1, further guide us to uncover novel mechanisms of oncogenic activation and corresponding treatment strategies. Collectively, rare and ultrarare genomic events are driving precision oncology toward an increasingly individualized era of "ultraprecision" cancer therapy. See related article by Zheng et al., p. 1573. - Source: PubMed
Le XiuningWolf Jürgen - The functional plasticity of tumor-associated macrophages (TAMs) is a critical determinant of the immunosuppressive microenvironment in cervical cancer, yet its integration into actionable prognostic frameworks remains limited. This study aimed to establish a TAM polarization-centered model and elucidate the mechanisms of underlying tumor-immune crosstalk. - Source: PubMed
Publication date: 2026/07/17
Chen YushaWang LingLi SuyuHuang JimiaoZhu LeileiHuang XiqiZheng XiangqinPan DilingHuang Chuanzhong - To investigate the mechanisms underlying benzo[a]pyrene-induced esophageal cancer (EC), and to screen and identify the key targets and biomarkers associated with benzo[a]pyrene-related EC. - Source: PubMed
Publication date: 2026/07/15
Lan XuyanHuang ZuqiangLin YukunSun XiaoyuGuo BinghanLi GenglinWang JintaoLin JinlanZhu LihuanGuo Tianxing - Resistance to FLT3 inhibitors remains a major limitation in the treatment of FLT3-mutated acute myeloid leukemia (AML). Canonically, ERK is considered the predominant MAPK effector downstream of FLT3 signaling. However, pharmacologic inhibition of MEK/ERK provides limited clinical benefit once resistance develops, suggesting that alternative signaling dependencies may emerge under therapeutic pressure. Using an unbiased kinome-wide CRISPR-Cas9 screen in gilteritinib-resistant AML cells, we identified MAPK14 (encoding p38α), rather than MAPK3/MAPK1 (encoding ERK1/2), as a prominent context-dependent dependency associated with the resistant state. Genetic impairment or pharmacologic inhibition of p38 enhanced gilteritinib sensitivity and synergized with FLT3 inhibition to suppress leukemic growth. Mechanistically, resistant cells exhibited adaptor-mediated rewiring of FLT3 signaling, in which p46-SHC1 supported an FLT3-associated MKK3/6-p38 signaling module despite FLT3 inhibition, thereby sustaining downstream programs including MYC expression. Consistent with its role as a stress-responsive kinase, p38 supports leukemic cell survival under prolonged drug exposure. Together, these findings define a non-canonical MAPK signaling state associated with FLT3 inhibitor resistance, provide a mechanistic explanation for the limited efficacy of MEK/ERK-directed therapies in the resistant setting, and offer a rationale for combination strategies targeting stress-adaptive pathways to improve the durability of FLT3-directed therapy in AML. - Source: PubMed
Publication date: 2026/07/29
Shen LongFan JintingWang NingWang ZihaoYang YangXu ChenghuaLiu SiyiZhang DongFang YouyangChu BingqianZhang TingtingLiu WenshuoKang LichunZhou ZhiweiNiu MingmingWang Hong