KCTD10 antibody - N-terminal region (ARP35370_T100)
- Known as:
- KCTD10 (anti-) - N-terminal region (ARP35370_T100)
- Catalog number:
- arp35370_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- KCTD10 antibody - N-terminal region (ARP35370_T100)
Related genes to: KCTD10 antibody - N-terminal region (ARP35370_T100)
- Gene:
- KCTD10 NIH gene
- Name:
- potassium channel tetramerization domain containing 10
- Previous symbol:
- -
- Synonyms:
- MSTP028, BTBD28
- Chromosome:
- 12q24.11
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-28
- Date modifiied:
- 2019-02-21
Related products to: KCTD10 antibody - N-terminal region (ARP35370_T100)
Related articles to: KCTD10 antibody - N-terminal region (ARP35370_T100)
- Transcription-replication conflicts (TRCs) are an increasingly recognized driver of genome instability in human cells. We recently identified the CUL3 adaptor KCTD10 as a sensor of co-directional TRCs, recruiting CUL3 to ubiquitinate transcriptional machinery and clear the path for replication forks. Here, we discuss the implications of this conflict-resolution pathway for human cancer. By integrating our mechanistic findings with large-scale functional genomics datasets, we identify oncogenic conditions that potentially create TRC-rich environments and render cells selectively dependent on KCTD10. These contexts reveal new mechanistic insights and potential therapeutic opportunities across a range of human cancers. - Source: PubMed
Publication date: 2026/03/04
Kloeber Jake AChen BinMutter RobertHuang JinzhouLou Zhenkun - Atherosclerotic cardiovascular disease (ASCVD) remains a leading cause of death worldwide, with plaque instability being a major culprit. Phenotypic switching of vascular smooth muscle cells (VSMCs) is a central event in atherosclerosis, driving both plaque progression and stability, yet the underlying mechanisms are incompletely understood, limiting drug development targeting this process. Kinesin family member 13B (KIF13B) has been implicated in vascular biology, but its function in VSMCs is unknown. Here, we demonstrate that VSMC-specific deletion of Kif13b in mice overexpressing proprotein convertase subtilisin/kexin type 9 (PCSK9) exacerbates lesion development and impairs plaque stability, characterized by thinner fibrous caps and increased inflammation. Mechanistically, we determined that KIF13B facilitated the ubiquitination and proteasomal degradation of Krüppel-like factor 4 (KLF4) through the potassium channel tetramerization domain-containing 10-dependent (KCTD10-dependent) pathway. This KIF13B/KCTD10 axis reduced KLF4 protein levels, thereby inhibiting the proinflammatory responses and fibroblast-like transition of VSMCs to preserve their contractile phenotype. Importantly, the adverse effects of Kif13b deficiency on atherogenesis were effectively rescued by the small-molecule KLF4 inhibitor Kenpaullone. Our results unveil a VSMC-specific atheroprotective role for KIF13B, define the KIF13B/KCTD10/KLF4 pathway as a key regulatory axis governing VSMC fate and plaque stability, and validate the therapeutic potential of KIF13B for treating advanced atherosclerosis. - Source: PubMed
Publication date: 2026/01/29
Miao GuolinHan YufeiChen JingxuanLiu YiranZhang GePei ShaotongZhao YinqiXu YitongZheng LiwenLi ZhaolingLiu XiangruShi SijingKang XuyaLiu YahanZhang LingHuang WeiWang YuhuiTang JunnanDong ErdanXian Xunde - Potassium channel tetramerization domain-containing 10 (KCTD10) plays a crucial role in the progression of various tumors. However, comprehensive studies on the involvement of KCTD10 in breast cancer are still lacking. This research aims to elucidate the potential roles and mechanisms of KCTD10 in breast cancer. Reduced KCTD10 expression was observed in breast cancer and was associated with poorer overall survival. Upregulation of KCTD10 resulted in a significant decline in cell growth and proliferation. Notably, KCTD10 overexpression induced ferroptosis, as evidenced by increased cell death, elevated ferrous ion levels, and enhanced lipid peroxidation. The anti-tumor effects mediated by KCTD10 elevation were significantly counteracted by ferroptosis inhibitors, while KCTD10 knockdown resulted in increased resistance to this form of cell death. KCTD10 overexpression reduced the protein levels of SLC7A11, a process reversible by proteasome inhibitors. In KCTD10 knockdown cells, the degradation rate of SLC7A11 protein was significantly decreased. Notably, restoring SLC7A11 expression in KCTD10-overexpressing cells significantly counteracted the tumor-suppressive effects of KCTD10. Tumor-bearing mouse models demonstrated that KCTD10-overexpressing cells exhibited significantly reduced tumor formation capabilities, accompanied by increased ferroptosis levels in tumor tissues. Collectively, KCTD10 exerts a vital anti-cancer role in breast cancer by promoting the ubiquitin-proteasome degradation of SLC7A11, which reduces GSH synthesis, limits the inhibition of lipid peroxidation, and ultimately triggers ferroptosis. By providing new insights into the molecular mechanisms underlying breast cancer pathogenesis, this research identifies KCTD10 as a valuable therapeutic target and suggests that gene therapies aimed at restoring its expression may offer promising avenues for breast cancer treatment. - Source: PubMed
Publication date: 2026/01/22
He XinWang YingWang DanWang LirongYu ShanshanJiang JueZhou Qi - During DNA replication, the replisome must remove barriers and roadblocks including the transcription machinery. Transcription-replication conflicts (TRCs) occur when there are collisions between the replisome and transcription machinery, and are increasingly recognized as an important source of mammalian genome instability. How cells facilitate replisome bypass at sites of TRCs is incompletely understood. Here we show that the CUL3-KCTD10 E3 ligase senses TRCs and promotes remodelling of the RNA polymerase complex to allow replisome bypass. We found that the substrate adaptor KCTD10 interacts with the replisome and the transcription machinery and regulates both in unstressed conditions. These bivalent interactions allow KCTD10 to detect co-directional TRCs and facilitate higher-order assembly of KCTD10 complexes that recruit CUL3 to induce the ubiquitination and removal of the RNA polymerase factor TCEA2. In the absence of KCTD10, there is increased retention of TCEA2 and the RNA polymerase complex, causing an accumulation of TRCs and increased DNA damage. Our results demonstrate how replication can proceed through transcriptionally active regions, utilizing a unique bridging function of the CUL3-KCTD10 complex. These findings provide a framework for how the coordination between transcription and replication may contribute to the maintenance of genome stability. - Source: PubMed
Publication date: 2025/10/08
Kloeber Jake AChen BinSun GuangchaoKing Charles SWang ZhiquanWang LiWu ZhemingZhu ShouhaiZhao FeiQin HongranOuyang YaobinXiao HuapingTu XinyiLu JingJiang YanxiaLuo KuntianYin PingWu XinyanMutter Robert WHuang JinzhouLou Zhenkun - Lung cancer remains a critical global health concern, characterized by the highest incidence and mortality rates among all cancers. Due to its heterogeneity and complexity, the molecular mechanism underlying lung cancer occurrence and progression needs to be further investigated. KCTD10 has been implicated in malignant phenotypes of several tumors, but the role of KCTD10 in lung cancer remains largely unexplored. In this study, we found that KCTD10 expression is significantly reduced in lung cancer tissues, and overexpression of KCTD10 could inhibit lung cancer progression both and . Immunoprecipitation-mass spectrometry (IP-MS), co-immunoprecipitation (Co-IP), and ubiquitination assays revealed that the BTB domain of KCTD10 interacts with Armadillo repeat domains 1-9 of β-catenin and facilitates ubiquitin-dependent degradation of β-catenin via the K48-linked ubiquitin chains, followed by the downregulation of the β-catenin downstream target gene PD-L1. Notably, the combined treatment of KCTD10 overexpression with anti-PD-1 antibodies exhibited a synergistic effect in suppressing lung cancer progression and brain metastatic colonization in mice. In addition, vascular endothelial cell-specific knockout of Kctd10 (Kctd10CDH5) promoted lung cancer metastasis and tumor angiogenesis through β-catenin signaling. Finally, we identified METTL14- mediated N6-methyladenosine (mA) modification within the coding sequence (CDS) region of KCTD10, which enhanced KCTD10 mRNA stability in a YTHDF2-dependent manner. These findings highlight KCTD10 as a critical regulator of lung cancer progression and the tumor microenvironment, suggesting its potential as a promising therapeutic target for lung cancer. - Source: PubMed
Publication date: 2025/08/12
Yin ZihaoLong ShengwenZhou HaoOuyang MiWang QinghaoHe JunSu RongyuLi ZhiweiDing XiaofengXiang Shuanglin