FBXW11 (BTRCP2) Antibody (OARA03203)
- Known as:
- FBXW11 (BTRCP2) Antibody (OARA03203)
- Catalog number:
- oara03203
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- FBXW11 (BTRCP2) Antibody (OARA03203)
Related genes to: FBXW11 (BTRCP2) Antibody (OARA03203)
- Gene:
- FBXW11 NIH gene
- Name:
- F-box and WD repeat domain containing 11
- Previous symbol:
- FBXW1B
- Synonyms:
- KIAA0696, Fbw1b, BTRCP2, BTRC2, Hos, Fbw11
- Chromosome:
- 5q35.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-09-27
- Date modifiied:
- 2015-09-11
Related products to: FBXW11 (BTRCP2) Antibody (OARA03203)
Related articles to: FBXW11 (BTRCP2) Antibody (OARA03203)
- Hair follicle stem cells (HFSCs) reside in a relatively hypoxic niche and preferentially use glycolytic metabolism, but how metabolic adaptation is coupled to epigenetic regulation of HFSC function remains incompletely understood. Since oxidative phosphorylation produces more reactive oxygen species (ROS) than glycolysis, and excessive ROS production eliminates various stem cell properties including quiescence and self-renewal. Stem cells prefer glycolysis as their main energy source. Here, cultured human HFSCs were exposed to 2%O. Hypoxia increased HIF-1α expression, glycolysis-related gene expression, intracellular H3K18 histone lactylation (H3K18la), EdU incorporation, colony-forming efficiency, and HFSC-associated markers CK15, CK19, and CD34 expression. Separate treatment with the glycolysis inhibitors 2-deoxy-D-glucose (2-DG) or oxamate reduced lactate accumulation, H3K18la, and HFSC-associated marker expression. Integrated H3K18la CUT&Tag and RNA sequencing identified 822 genes with concordantly increased H3K18la peaks and mRNA levels, with ubiquitin-mediated proteolysis among the enriched pathways. FBXW11 was prioritized as a candidate E3 ubiquitin ligase target. IGV visualization and H3K18la ChIP-qPCR showed increased H3K18la enrichment at the FBXW11 locus under hypoxia, whereas 2-DG or the p300 inhibitor C646 attenuated H3K18la enrichment and FBXW11 expression. FBXW11 overexpression increased EdU incorporation, colony formation, and HFSC-associated marker expression, while FBXW11 knockdown attenuated hypoxia-induced clonogenic growth and proliferation. In an ex vivo whole-hair-follicle culture model, hypoxia enhanced hair shaft elongation, and this effect was reduced by FBXW11 knockdown. Together, these findings support a hypoxia-glycolysis/lactate-H3K18la-FBXW11 pathway that contributes to proliferative and self-renewal-associated phenotypes of cultured HFSCs and to hypoxia-responsive hair shaft growth ex vivo. Further in vivo studies are required to establish its role in physiological hair cycle. - Source: PubMed
Publication date: 2026/09/23
Guanyu LinXuejun NiChen LeiXiuying ShanBiao Wang - Ubiquitination regulation is essential for maintaining protein homeostasis. Dysregulated ubiquitination is increasingly recognized to participate in malignant progression. Fbxw11, a substrate-recognition subunit of SCF-type E3 ligases, is involved in tumorigenesis and progression. However, its role and molecular mechanism in acute myeloid leukemia (AML) have not been elucidated. Here we demonstrat that lower levels of Fbxw11 were detected in AML patients and correlated with worse prognosis. Furthermore, overexpression of Fbxw11 delayed AML progression by reducing leukemia stem cell (LSC) frequency and inhibiting leukemia cell migration. Mechanistically, quantitative proteomics combined with co-immunoprecipitation and ubiquitination assays identified dihydropyrimidinase-like 2 (Dpysl2) as a direct substrate of Fbxw11, leading to its poly-ubiquitylation and proteasomal degradation. Moreover, overexpression of Dpysl2 reversed the effects of Fbxw11 on LSC levels and migration of AML cells as well as accelerated AML progression in vivo. In addition, inhibition of Dpysl2 with lacosamide, an FDA-approved antiepileptic drug, phenocopied Fbxw11 restoration and delayed AML progression. Lacosamide combined with cytarabine further prolonged the survival of AML mice. Our results suggest Fbxw11 as an intrinsic suppressor in AML progression by regulating the ubiquitination and degradation of Dpysl2, providing new insights into ubiquitination regulation and highlighting the potential of targeting the Fbxw11-Dpysl2 axis as a therapeutic strategy for AML. - Source: PubMed
Publication date: 2026/08/12
Wang LinaLi YifeiXie WanzhenLi RuiyunCui XiaoxiZhang SiqiRen QianZheng Guoguang - Pancreatic ductal adenocarcinoma (PDAC) is characterized by a pronounced Warburg effect and high lactate levels. While lysine lactylation (Kla) is an emerging post-translational modification, its role in regulating the S100A11/ANXA2 complex-a critical driver of membrane repair and metastasis-remains unexplored. In this study, we identified that S100A11 (K3, K55) and ANXA2 (K49) are significantly lactylated in PDAC tissues. Lactate-induced lactylation of S100A11 at K3 and K55 inhibits FBXW11-mediated ubiquitination and proteasomal degradation, thereby stabilizing the protein. This stabilized S100A11 subsequently shields ANXA2 from TRIM21-mediated degradation. Reciprocally, lactylation of ANXA2 at K49 enhances its capacity to recruit S100A11 to the plasma membrane. Functional assays demonstrated that this lactylation-driven interdependent regulatory axis promotes PDAC cell migration, invasion, and metastasis both in vitro and in vivo. Clinical analysis of TCGA data revealed that low expression of both S100A11 and ANXA2 predicts significantly improved progression-free and overall survival in PDAC patients. In summary, our findings establish a novel link between metabolic reprogramming and the post-translational regulation of the membrane repair machinery. Lactylation of the S100A11/ANXA2 axis is a key driver of PDAC progression and serves as a promising prognostic biomarker and potential therapeutic target. - Source: PubMed
Publication date: 2026/07/10
Zheng BoCai LijunDeng YingYang Lan - Protein lactylation, a novel post-translational modification utilizing lactate as the substrate, has emerged as a key mechanism linking metabolic alterations to cancer progression. This study aims to investigate the role and underlying mechanism of S100A11 lactylation in gastric cancer progression and metastasis. - Source: PubMed
Publication date: 2026/07/09
Zhang QingruiZhou YuhangWang FangningYan JingruiLiu JiayuZhang LinDu Shiyu - Despite the well-established role of interleukin-17 (IL-17)-producing γδ T cells (γδT17 cells) in autoimmune inflammations, key factors to trigger the activation of γδT17 cells remain largely unknown. Here, we show that aryl hydrocarbon receptor (AhR) is markedly reduced upon γδT17 cell activation. AhR deficiency and pharmacological activation promotes and suppresses γδT17 cell activation, respectively. Mechanistically, AhR deficiency strengthens heat shock protein family A member 9 (HSPA9)-mediated competition with F-box and WD-40 domain protein 11(FBXW11) for binding to RBP-j-associated molecule (RAM) domain of Notch intracellular domain (NICD), which impairs FBXW11-dependent NICD ubiquitination to increase NICD occupancy at the enhancer to drive γδT17 cell activation. Consistently, AhR deficiency increases the proportion of γδT17 cells and the disease severity in psoriasis-like dermatitis mice and colitis mice, which is almost entirely reversed by pretreatment with either adeno-associated virus (AAV)-sh or AAV-sh. Collectively, these findings identify AhR deficiency as a key driver of aberrant γδT17 activation, uncover a γδT17 activation mechanism via HSPA9/FBXW11-mediated suppression of NICD ubiquitination, and provide a strong mechanistic basis for AhR agonists as therapeutics in autoimmune inflammations. - Source: PubMed
Publication date: 2026/07/03
He YueGuo YileiShi YuxinWan XuanmingZhu YanrongZhang WenjieLin HaochangWei ZhifengXia YufengDai Yue