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U.S.A."],"published-print":{"date-parts":[[2019,7,23]]},"abstract":"<jats:p>\n                    O-GlcNAc transferase (OGT) is an X-linked gene product that is essential for normal development of the vertebrate embryo. It catalyses the O-GlcNAc posttranslational modification of nucleocytoplasmic proteins and proteolytic maturation of the transcriptional coregulator Host cell factor 1 (HCF1). Recent studies have suggested that conservative missense mutations distal to the OGT catalytic domain lead to X-linked intellectual disability in boys, but it is not clear if this is through changes in the O-GlcNAc proteome, loss of protein\u2013protein interactions, or misprocessing of HCF1. Here, we report an OGT catalytic domain missense mutation in monozygotic female twins (c. X:70779215 T &gt; A, p. N567K) with intellectual disability that allows dissection of these effects. The patients show limited IQ with developmental delay and skewed X-inactivation. Molecular analyses revealed decreased OGT stability and disruption of the substrate binding site, resulting in loss of catalytic activity. Editing this mutation into the\n                    <jats:italic>Drosophila<\/jats:italic>\n                    genome results in global changes in the O-GlcNAc proteome, while in mouse embryonic stem cells it leads to loss of O-GlcNAcase and delayed differentiation down the neuronal lineage. These data imply that catalytic deficiency of OGT could contribute to X-linked intellectual disability.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1900065116","type":"journal-article","created":{"date-parts":[[2019,7,11]],"date-time":"2019-07-11T19:35:15Z","timestamp":1562873715000},"page":"14961-14970","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":92,"title":["Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability"],"prefix":"10.1073","volume":"116","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0081-9310","authenticated-orcid":false,"given":"Veronica M.","family":"Pravata","sequence":"first","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Villo","family":"Muha","sequence":"additional","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mehmet","family":"Gundogdu","sequence":"additional","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew T.","family":"Ferenbach","sequence":"additional","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Poonam S.","family":"Kakade","sequence":"additional","affiliation":[{"name":"Division of Cell and Developmental Biology, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vasudha","family":"Vandadi","sequence":"additional","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ariane C.","family":"Wilmes","sequence":"additional","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir S.","family":"Borodkin","sequence":"additional","affiliation":[{"name":"Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shelagh","family":"Joss","sequence":"additional","affiliation":[{"name":"West of Scotland Genetic Service, Queen Elizabeth University Hospital, G51 4TF Glasgow, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marios P.","family":"Stavridis","sequence":"additional","affiliation":[{"name":"Division of Cell and Developmental Biology, School of Life Sciences, University of Dundee, DD1 5EH Dundee, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daan M. 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Chem."},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.1046\/j.1471-4159.2001.00655.x","article-title":"Cytosolic O-glycosylation is abundant in nerve terminals","volume":"79","author":"Cole R. N.","year":"2001","unstructured":"R. N. Cole, G. W. Hart, Cytosolic O-glycosylation is abundant in nerve terminals. J. Neurochem. 79, 1080\u20131089 (2001).","journal-title":"J. Neurochem."},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1074\/mcp.T500040-MCP200","article-title":"O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry","volume":"5","author":"Vosseller K.","year":"2006","unstructured":"K. Vosseller ., O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 5, 923\u2013934 (2006).","journal-title":"Mol. Cell. 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