{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T03:04:18Z","timestamp":1790910258312,"version":"4.1.0"},"reference-count":71,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2022,10,17]],"date-time":"2022-10-17T00:00:00Z","timestamp":1665964800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 GM129324"],"award-info":[{"award-number":["R01 GM129324"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R24 GM134210"],"award-info":[{"award-number":["R24 GM134210"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["S10 OD021728"],"award-info":[{"award-number":["S10 OD021728"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,4,19]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>O-GlcNAcylation is a prominent modification of nuclear and cytoplasmic proteins in animals and plants and is mediated by a single O-GlcNAc transferase (OGT). Spindly (Spy), a paralog of OGT first discovered in higher plants, has an ortholog in the apicomplexan parasite Toxoplasma gondii, and both enzymes are now recognized as O-fucosyltransferases (OFTs). Here we investigate the evolution of spy-like genes and experimentally confirm OFT activity in the social amoeba Dictyostelium\u2014a protist that is more related to fungi and metazoa. Immunofluorescence probing with the fucose-specific Aleuria aurantia lectin (AAL) and biochemical cell fractionation combined with western blotting suggested the occurrence of nucleocytoplasmic fucosylation. The absence of reactivity in mutants deleted in spy or gmd (unable to synthesize GDP-Fuc) suggested monofucosylation mediated by Spy. Genetic ablation of the modE locus, previously predicted to encode a GDP-fucose transporter, confirmed its necessity for fucosylation in the secretory pathway but not for the nucleocytoplasmic proteins. Affinity capture of these proteins combined with mass spectrometry confirmed monofucosylation of Ser and Thr residues of several known nucleocytoplasmic proteins. As in Toxoplasma, the Spy OFT was required for optimal proliferation of Dictyostelium under laboratory conditions. These findings support a new phylogenetic analysis of OGT and OFT evolution that indicates their occurrence in the last eukaryotic common ancestor but mostly complementary presence in its eukaryotic descendants with the notable exception that both occur in red algae and plants. Their generally exclusive expression, high degree of conservation, and shared monoglycosylation targets suggest overlapping roles in physiological regulation.<\/jats:p>","DOI":"10.1093\/glycob\/cwac071","type":"journal-article","created":{"date-parts":[[2022,10,17]],"date-time":"2022-10-17T11:00:38Z","timestamp":1666004438000},"page":"225-244","source":"Crossref","is-referenced-by-count":6,"title":["<i>Spindly<\/i> is a nucleocytosolic <i>O<\/i>-fucosyltransferase in <i>Dictyostelium<\/i> and related proteins are widespread in protists and bacteria"],"prefix":"10.1093","volume":"33","author":[{"given":"Hanke","family":"van der Wel","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Georgia , Athens, GA 30602 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Maria","family":"Garcia","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center , Oklahoma City, OK 73104 , USA"},{"name":"Obstetrics and Gynecology (OBGYN) , 1951 SW 172nd Ave, Hollywood, FL 33029 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisabet","family":"Gas-Pascual","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Georgia , Athens, GA 30602 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Macy M","family":"Willis","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Georgia , Athens, GA 30602 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyun W","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Georgia , Athens, GA 30602 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giulia","family":"Bandini","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Henry Goldman School of Dental Medicine , Boston, MA 02118 , USA"},{"name":"Clarivate Analytics (UK) Ltd. , 70 St. Mary Axe, London, EC3A 8BE"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maissa Mareme","family":"Gaye","sequence":"additional","affiliation":[{"name":"Department of Biochemistry , Center for Biomedical Mass Spectrometry, , Boston, MA 02118 , USA"},{"name":"Boston University School of Medicine , Center for Biomedical Mass Spectrometry, , Boston, MA 02118 , USA"},{"name":"Chemistry Technology Center , Waters Corporation, Milford, MA 01757 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine E","family":"Costello","sequence":"additional","affiliation":[{"name":"Department of Biochemistry , Center for Biomedical Mass Spectrometry, , Boston, MA 02118 , USA"},{"name":"Boston University School of Medicine , Center for Biomedical Mass Spectrometry, , Boston, MA 02118 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Samuelson","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Henry Goldman School of Dental Medicine , Boston, MA 02118 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher M","family":"West","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology , Center for Tropical and Emerging Global Diseases, Complex Carbohydrate Research Center, , Athens, GA 30602 , USA"},{"name":"University of Georgia , Center for Tropical and Emerging Global Diseases, Complex Carbohydrate Research Center, , Athens, GA 30602 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2022,10,17]]},"reference":[{"key":"2023041913031816600_ref1","doi-asserted-by":"crossref","first-page":"11567","DOI":"10.1073\/pnas.1613653113","article-title":"O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii","volume":"113","author":"Bandini","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2023041913031816600_ref2","doi-asserted-by":"crossref","first-page":"1967","DOI":"10.1074\/jbc.RA118.005179","article-title":"O-Fucosylation of thrombospondin-like repeats is required for processing of microneme protein 2 and for efficient host cell invasion by Toxoplasma gondii tachyzoites","volume":"294","author":"Bandini","year":"2019","journal-title":"J Biol Chem"},{"key":"2023041913031816600_ref3","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.RA120.015883","article-title":"The nucleocytosolic O-fucosyltransferase Spindly affects protein expression and virulence in Toxoplasma gondii","volume":"296","author":"Bandini","year":"2021","journal-title":"J Biol Chem"},{"key":"2023041913031816600_ref4","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1093\/glycob\/cwn107","article-title":"Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum","volume":"19","author":"Banerjee","year":"2009","journal-title":"Glycobiology"},{"key":"2023041913031816600_ref5","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1007\/978-1-62703-302-2_15","article-title":"Isolation of Dictyostelium nuclei for light and electron microscopy","volume":"983","author":"Batsios","year":"2013","journal-title":"Meth Mol Biol"},{"key":"2023041913031816600_ref6","doi-asserted-by":"crossref","first-page":"e02445","DOI":"10.1128\/mBio.02445-14","article-title":"Systems-based analysis of the Sarcocystis neurona genome identifies pathways that 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