{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Howard TR"],"funding":["Edward Mallinckrodt, Jr. Foundation","Edward Mallinckrodt, Jr. Foundation (EMF)","HHS | NIH | National Institute of General Medical Sciences","NIAID NIH HHS","HHS | NIH | National Institute of Allergy and Infectious Diseases","HHS | NIH | National Institute of General Medical Sciences (NIGMS)","NIGMS NIH HHS","Princeton Catalysis Initiative","HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID)"],"pagination":["e0039721"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8269231"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(3)"],"pubmed_abstract":["DNA sensors are critical components of innate immunity that enable cells to recognize infection by pathogens with DNA genomes. The interferon-inducible protein X (IFIX), a member of the PYHIN protein family, is a DNA sensor capable of promoting immune signaling after binding to double-stranded DNA (dsDNA) within either the nucleus or cytoplasm. Here, we investigate the impact of IFIX on the cellular proteome upon introduction of foreign DNA to the nucleus or the cytoplasm as well as regulatory hubs that control IFIX subcellular localization. Using quantitative mass spectrometry, we define the effect of CRISPR-mediated IFIX knockout on nuclear and cytoplasmic proteomes in fibroblasts. Proteomes are probed in response to either nuclear viral DNA, during herpes simplex virus 1 (HSV-1) infecti"],"journal":["mSystems"],"pubmed_title":["The DNA Sensor IFIX Drives Proteome Alterations To Mobilize Nuclear and Cytoplasmic Antiviral Responses, with Its Acetylation Acting as a Localization Toggle."],"pmcid":["PMC8269231"],"funding_grant_id":["F31 AI114240","T32 GM007388","T32GM007388","F31 GM120936","AI114240","GM114141","GM120936","R01 GM114141"],"pubmed_authors":["Crow MS","Li T","Cristea IM","Howard TR","Greco TM","Lum KK"],"additional_accession":[]},"is_claimable":false,"name":"The DNA Sensor IFIX Drives Proteome Alterations To Mobilize Nuclear and Cytoplasmic Antiviral Responses, with Its Acetylation Acting as a Localization Toggle.","description":"DNA sensors are critical components of innate immunity that enable cells to recognize infection by pathogens with DNA genomes. The interferon-inducible protein X (IFIX), a member of the PYHIN protein family, is a DNA sensor capable of promoting immune signaling after binding to double-stranded DNA (dsDNA) within either the nucleus or cytoplasm. Here, we investigate the impact of IFIX on the cellular proteome upon introduction of foreign DNA to the nucleus or the cytoplasm as well as regulatory hubs that control IFIX subcellular localization. Using quantitative mass spectrometry, we define the effect of CRISPR-mediated IFIX knockout on nuclear and cytoplasmic proteomes in fibroblasts. Proteomes are probed in response to either nuclear viral DNA, during herpes simplex virus 1 (HSV-1) infecti","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2026-06-12T03:25:28.875Z","creation":"2024-10-18T22:40:56.73Z"},"accession":"S-EPMC8269231","cross_references":{"pubmed":["34156286"],"doi":["10.1128/mSystems.00397-21"]}}