{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Unoki M"],"funding":["Japan Society for Promotion of Science"],"pagination":["1575-1583"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11373322"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(18)"],"pubmed_abstract":["We have recently discovered that the so-called subcortical maternal complex (SCMC) proteins composing of cytoplasmic lattices are destabilized in Uhrf1 knockout murine fully grown oocytes (FGOs). Here we report that human UHRF1 interacts with human NLRP5 and OOEP, which are core components of the SCMC. Moreover, NLRP5 and OOEP interact with DPPA3, which is an essential factor for exporting UHRF1 from the nucleus to the cytoplasm in oocytes. We identify that NLRP5, not OOEP, stabilizes UHRF1 protein in the cytoplasm utilizing specifically engineered cell lines mimicking UHRF1 status in oocytes and preimplantation embryos. Further, UHRF1 is destabilized both in the cytoplasm and nucleus of Nlrp5 knockout murine FGOs. Since pathogenic variants of the SCMC components frequently cause multilocu"],"journal":["Human molecular genetics"],"pubmed_title":["The maternal protein NLRP5 stabilizes UHRF1 in the cytoplasm: implication for the pathogenesis of multilocus imprinting disturbance."],"pmcid":["PMC11373322"],"funding_grant_id":["JP19H05740","JP18H05214","23K05728","13K05728"],"pubmed_authors":["Unoki M","Uemura S","Fujimoto A","Sasaki H"],"additional_accession":[]},"is_claimable":false,"name":"The maternal protein NLRP5 stabilizes UHRF1 in the cytoplasm: implication for the pathogenesis of multilocus imprinting disturbance.","description":"We have recently discovered that the so-called subcortical maternal complex (SCMC) proteins composing of cytoplasmic lattices are destabilized in Uhrf1 knockout murine fully grown oocytes (FGOs). Here we report that human UHRF1 interacts with human NLRP5 and OOEP, which are core components of the SCMC. Moreover, NLRP5 and OOEP interact with DPPA3, which is an essential factor for exporting UHRF1 from the nucleus to the cytoplasm in oocytes. We identify that NLRP5, not OOEP, stabilizes UHRF1 protein in the cytoplasm utilizing specifically engineered cell lines mimicking UHRF1 status in oocytes and preimplantation embryos. Further, UHRF1 is destabilized both in the cytoplasm and nucleus of Nlrp5 knockout murine FGOs. Since pathogenic variants of the SCMC components frequently cause multilocu","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-06-01T17:40:43.341Z","creation":"2025-04-05T22:13:26.369Z"},"accession":"S-EPMC11373322","cross_references":{"pubmed":["38868925"],"doi":["10.1093/hmg/ddae096"]}}