Ask about this productRelated genes to: MCM9 Blocking Peptide
- Gene:
- MCM9 NIH gene
- Name:
- minichromosome maintenance 9 homologous recombination repair factor
- Previous symbol:
- MCMDC1, C6orf61
- Synonyms:
- MGC35304, dJ329L24.3, FLJ20170
- Chromosome:
- 6q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-18
- Date modifiied:
- 2015-08-25
Related products to: MCM9 Blocking Peptide
Related articles to: MCM9 Blocking Peptide
- Primary liver cancer ranks among the most prevalent and refractory malignant tumors globally. This investigation delves into the role of Epstein-Barr virus nuclear antigen 2-binding protein (EBP2) in hepatocellular carcinoma (HCC). Significantly, EBP2 exhibits marked overexpression in HCC tissues, a finding that correlates with advanced tumor staging and unfavorable prognostic outcomes. In HCC cells, EBP2 silencing led to attenuated proliferation, enhanced apoptosis, and reduced migratory capacity, coupled with reversal of epithelial-mesenchymal transition (EMT). In vivo studies further demonstrated that EBP2 depletion potently suppressed tumor growth in xenograft models. Mechanistically, EBP2 interacts with CENPA to transcriptionally upregulate minichromosome maintenance protein family member 8 (MCM8), thereby stabilizing the MCM8/MCM9 complex and enhancing homologous recombination-mediated DNA repair. Functional rescue experiments revealed that MCM8 overexpression abrogated the suppressive effects of EBP2 knockdown on HCC cell proliferation and migration. In parallel, EBP2 regulates HMGB1 expression through the CENPA/YY1 transcriptional complex, thereby participating in the progression of HCC. Collectively, these findings highlight EBP2 as a crucial regulator of HCC progression via the dual axes-EBP2-CENPA-MCM8 and EBP2-CENPA/YY1-HMGB1, offering a promising therapeutic target for HCC intervention. - Source: PubMed
Publication date: 2026/04/04
Ma EnsiXing HaoSun ChaoZhang QuanbaoShen ConghuanZhan YangyangLi JianhuaLi LiXue HongyuanLi RuidongTeng FeiTao Yifeng - The Homologous Recombination Factor With OB-Fold (HROB) plays a role in homologous recombination and DNA replication, where it enhances the MCM8-MCM9 helicase complex activity. Recent findings link biallelic germline HROB variants to primary gonadal insufficiency (hypergonadotropic hypogonadism), a phenotype also associated with MCM8/MCM9 deficiency. Here, we describe a family where two individuals with biallelic HROB variants presented with hypergonadotropic hypogonadism and colonic polyposis. Exome sequencing identified three unique HROB variants: a likely pathogenic nonsense variant (c.1267C>T [p.(Gln423*)]) in exon four, and two missense variants (c.1363C>G [p.(Leu455Val)] and c.1318A>G [p.(Ser440Gly)]) in exon five. RNA analysis and protein mapping indicate that the nonsense variant is likely pathogenic, whereas the missense variants remain of uncertain significance. Mutational signature analysis of polyposis tissue did not reveal signatures directly linked to HROB deficiency, yet a review of published cases and analyses of cohorts with unexplained polyposis/cancer identified additional individuals with HROB variants exhibiting hypergonadotropic hypogonadism or colonic polyposis. These findings reinforce the association between biallelic germline HROB variants and hypergonadotropic hypogonadism and suggest a potential role in colonic polyposis predisposition. We recommend incorporating HROB into diagnostic gene panels for hypergonadotropic hypogonadism, especially in cases where colonic polyposis is also present. Furthermore, we emphasize the importance of additional studies to comprehensively characterize HROB's phenotypic impact and assess its contribution to disease risk. - Source: PubMed
Publication date: 2026/03/25
Helderman Noah CTops Carli MLegebeke JelmerYang TingGay Marcos DíazTerlouw DianthaLashley Lisa E E L OAretz StefanSommer Anna KTerradas MarionaValle Laurade Voer Richarda MAlexandrov Ludmil BMorreau Hansvan Wezel TomNielsen Maartje - - Source: PubMed
Publication date: 2025/12/18
Lutzmann MalikBernex Florenceda Costa de Jesus CindyHodroj DanaMarty CarolinePlo IsabelleVainchenker WilliamTosolini MarieForichon LucBret CarolineQueille SophieMarchive CandiceHoffmann Jean-SébastienMéchali Marcel - : Triple-negative breast cancer (TNBC) accounts for 15 to 20% of breast cancer cases and contributes to a disproportionate 35% of breast cancer deaths. Its resistance to chemotherapy presents a significant challenge. : We firstly compared transcriptomic profiles between TNBC cell lines and patient samples and inferred the MDA-MB-231 cell line as the most representative model for TNBC with poor response to chemotherapy. We then conducted a genome-wide CRISPR-Cas9 screening and RNA-seq analysis in MDA-MB-231. : This analysis revealed 96 and 93 genes that could re-sensitize cisplatin and doxorubicin treatment, respectively, with 19 overlapping genes. Among these genes, 28 have been studied and published previously in chemoresistance research. MCM9 was found as a new TNBC chemoresistance target. Its target drug, KPT-185, showed an additive effect with cisplatin in treating TNBC cells. In the follow-up gene combination double-knockout experiment among 65 genes selected from cell death pathways, 242 synthetic lethal gene pairs were discovered to overcome chemoresistance in TNBC. : In this study, we identified synthetic lethal targets in treating TNBC with cisplatin and doxorubicin through a genome-wide CRISPR-Cas9 screening and gene combination double-knockout screening. - Source: PubMed
Publication date: 2025/12/03
Shao ShuaiLi ShangjiaHuo YangTang ShanGökbağ BirkanFan KunjieHuang YiruiWang LinglingNagy GregoryParvin JeffreyStover DanielCheng LijunLi Lang - The Fanconi anemia (FA) protein FANCD2, and MCM8/9 heterohexameric helicase complex are critical for maintaining genomic integrity in response to replication stress, however, the nature of their relationship remains unclear. Here, we show that MCM8/9 interacts and functionally cooperates with FANCD2 within a complex during the repair of DNA interstrand crosslinks (ICLs). Using immunofluorescence and co-immunoprecipitation studies, we show that MCM8/9 interacts with the FANCD2 complex through its core domain. FANCD2 is essential for the recruitment of MCM8/9 to ICL damage induced nuclear foci but acts independently of FANCD2 monoubiquitination. Although MCM8/9 foci formation requires its intact ATPase activity, the BRCv motif within the MCM9 C-terminal extension (CTE) and the accessory protein, HROB, these are not required for FANCD2 binding, highlighting a distinction between physical interaction and functional activation. Interestingly, FANCD2 foci formation increases in MCM8 or MCM9 knockout cells or with knockdown of the activator, HROB, suggesting that MCM8/9 functions to mitigate replication-associated stress. γH2AX DNA damage assays and cell survival assays show that combined loss of MCM9 and FANCD2 do not cause additive DNA damage beyond individual knockouts, indicating an epistatic relationship of MCM8/9 with FANCD2, functioning in the same DNA repair pathway. Together, our findings identify MCM8/9 as a downstream interactor and effector of FANCD2/I critical for resolving ICL induced DNA damage. - Source: PubMed
Publication date: 2025/11/09
Beragama Arachchi Rashini YOkafor Desmond CSnyder Andrew JTrakselis Michael A