Ask about this productRelated genes to: EME1 Blocking Peptide
- Gene:
- EME1 NIH gene
- Name:
- essential meiotic structure-specific endonuclease 1
- Previous symbol:
- -
- Synonyms:
- FLJ31364, MMS4L, SLX2A
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-27
- Date modifiied:
- 2015-02-24
Related products to: EME1 Blocking Peptide
Related articles to: EME1 Blocking Peptide
- To investigate the genetic architecture of male genital lichen sclerosus (MGLSc) and to identify potential susceptibility loci, candidate genes, and biological pathways associated with disease pathogenesis by integrating genomic structural equation modeling (Genomic-SEM) with multi-omics analyses and experimental validation. - Source: PubMed
Publication date: 2026/07/16
Chen JianbaiZhang ZhimingFu QiangHou HaozhongXu GongquanLi ZhenyuLu ZhiguoQiu JianxinWu KeGao XiaopingZhang GengYang LongfeiSong RundongZhang Wei - Cervical cancer is mainly driven by persistent infection with high-risk human papillomaviruses (HPV), particularly HPV16 and HPV18. Despite advances in cytology, HPV-DNA testing and vaccination, challenges remain in the triage of HPV-positive individuals, prognostic stratification and prediction of treatment response. Non-coding RNAs (ncRNAs), including microRNAs, long non-coding RNAs and circular RNAs, together with host genetic factors influencing ncRNA expression and emerging lncRNA-encoded peptides, are increasingly recognized as regulators of HPV-associated carcinogenesis. This review summarizes their biological and potential clinical relevance. A structured literature search was conducted in PubMed and Scopus. Eligible studies included experimental, clinical, observational, genomic and translational investigations on ncRNA dysregulation, circulating or exosomal ncRNAs, treatment-response signatures, host genetic variation and lncRNA-encoded peptides in HPV-associated cervical precancer and cancer. HPV oncoproteins can reshape host ncRNA networks through transcriptional and epigenetic mechanisms. Several miRNAs, lncRNAs and circRNAs are involved in cell-cycle control, apoptosis, senescence, epithelial-mesenchymal transition, immune regulation, DNA repair and treatment resistance. Circulating, exosomal and urinary ncRNA signatures have shown diagnostic or prognostic potential in exploratory cohorts. Specific lncRNAs, including ENSG00000267838/lnc-LENG9-5 and lncRNA-EME1, have been associated with chemoradiotherapy response and radioresistance. The lncRNA-encoded peptide TUBORF represents a novel preclinical therapeutic candidate, while genetic variation may further modulate lncRNA function in HPV-related cervical cancer. ncRNAs are promising candidates for risk stratification, non-invasive diagnosis, treatment-response prediction and therapeutic development in HPV-associated cervical disease. However, evidence remains exploratory, requiring prospective multicentre validation and standardized workflows before clinical implementation. - Source: PubMed
Publication date: 2026/06/21
Terrinoni MatteoCaputo ValerioPalisciano MicheleMascellino GiuseppeGerli SandroFavilli Alessandro - SLX4 is a scaffold protein pivotal in genome protection mechanisms ranging from homologous recombination and interstrand cross-link (ICL) repair to mechanisms that deal with challenged DNA replication. Many of human SLX4 functions rely on its ability to interact and control the XPF-ERCC1, MUS81-EME1, and SLX1 structure-specific endonucleases. Interaction with MUS81 relies on the conserved SAP domain of SLX4. Since the same domain in yeast Slx4 orthologs does not interact with Mus81, we investigated whether human SLX4 SAP might have retained some ancestral MUS81-independent functions. We show that human SLX4 SAP binds DNA with a preference for branched structures such as Holliday junctions. We further discovered that phosphorylation of SLX4 SAP by CDK1, which promotes interaction with MUS81, inhibits DNA binding. We identified separation of function mutants that impair either DNA or MUS81 binding. Binding to MUS81 is required in response to ICL-inducing agents, methyl methanesulfonate (MMS), TOP1, and PARP inhibition. Instead, DNA binding is required in response to ICL-inducing agents and MMS but not after TOP1 or PARP inhibition. Our work indicates that phosphorylation by CDK1 acts as a regulatory switch between DNA binding and MUS81-dependent functions of SLX4, to accommodate specific DNA lesions or secondary structures. - Source: PubMed
Scaglione SarahGaillard Pierre-Henri - Recombinational repair provides an important pathway for the repair of DNA double strand breaks that arise in mitotic and meiotic cells. Homologous pairing and strand exchange leads to the formation of DNA intermediates that are linked by double Holliday junctions, and these need to be resolved prior to chromosome segregation and cell division. In mitotic cells, resolution occurs by either of two distinct pathways (i) Nucleolytic cleavage by GEN1 or SLX1-SLX4-MUS81-EME1-XPF-ERCC1 (SMX complex), or (ii) dissolution mediated by BLM-TopoIIIα-RMI1-RMI2 (BTRR complex). To facilitate the biochemical analysis of these pathways, we previously developed a novel methodology, involving DNAzyme self-cleavage, to generate 1.8-kb long DNA molecules containing dHJs. This involved the sequential annealing of precursor ssDNAs, which were first individually isolated through multiple rounds of gel purification and ethanol precipitation, but unfortunately the method was laborious and inefficient as considerable DNA losses were incurred at each step. Here, we describe a significantly improved methodology, that increases both the efficiency and yield without impacting the quality of the dHJs produced. The new method is rapid and simple, requiring only basic molecular biology expertise, and results in the formation of dHJs that make ideal substrates for the biochemical analysis of dissolution and resolution reaction in vitro. - Source: PubMed
Publication date: 2026/03/25
Shah Punatar RajveeHo Han NWest Stephen C - Faithful genome transmission depends on the timely removal of branched DNA intermediates. This task is executed by the SMX tri-nuclease, a mitosis-specific complex containing three structure-selective endonucleases (SLX1, MUS81-EME1, and XPF-ERCC1) bound to the SLX4 scaffold. A critical step in SMX assembly is the recruitment of MUS81-EME1 to SLX4 in early mitosis, a process tightly regulated by cell-cycle kinases. Mechanistically, CDK1-dependent phosphorylation of SLX4 promotes folding of its SAP domain, which strengthens the SLX4-MUS81 interaction. Here, we define a site-specific phosphorylation code that stabilizes complementary structures in the SLX4-MUS81 interface. Phosphorylation of SLX4 T1571 is required for partial SAP domain folding, pre-organizing the MUS81 binding surface and reducing the entropic penalty of folding upon binding. Co-phosphorylation at T1561 enhances structural stability and promotes intermolecular β-sheet formation with MUS81, providing enthalpic stabilization. Dual-site phosphorylation converts a relatively weak interaction into a high-affinity complex that stimulates MUS81-EME1 nuclease activity. In human cells, both phosphorylation sites are required for robust SMX assembly and genome stability maintenance. Collectively, our findings reveal the structural basis for how CDK1-cyclin B controls SMX assembly in mitosis. More broadly, the SLX4-MUS81 complex illustrates how phosphorylation fine-tunes marginally stable protein interfaces at the boundary of order and disorder. - Source: PubMed
Payliss Brandon JYun Hwa YoungDoshi SarinaLemak AlexanderTse Ying Wah EAprosoff Camila MHouliston ScottArrowsmith Cheryl HWyatt Haley D M