2020
Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation
Edani BH, Grabińska KA, Zhang R, Park EJ, Siciliano B, Surmacz L, Ha Y, Sessa WC. Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 20794-20802. PMID: 32817466, PMCID: PMC7456142, DOI: 10.1073/pnas.2008381117.Peer-Reviewed Original ResearchConceptsActive site tunnelProtein glycosylationAtomic resolution structuresGlycosyl carrier lipidsΑ3 helixEnzyme active sitePTase activityResolution structureActive siteEndoplasmic reticulumHomodimeric formCarrier lipidRate-limiting stepGlycosylationCrystal structureDHDDSStructural elucidationPTaseIsoprene chainPrenyltransferaseUnique insightsComplexesUnfavorable stateNgBRHomodimeric
2017
A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity
Grabińska KA, Edani BH, Park EJ, Kraehling JR, Sessa WC. A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity. Journal Of Biological Chemistry 2017, 292: 17351-17361. PMID: 28842490, PMCID: PMC5655512, DOI: 10.1074/jbc.m117.806034.Peer-Reviewed Original ResearchMeSH KeywordsAlkyl and Aryl TransferasesAmino Acid MotifsBacterial ProteinsDimethylallyltranstransferaseFungal ProteinsHumansPlant ProteinsReceptors, Cell SurfaceTransferasesConceptsUndecaprenyl diphosphate synthaseDiphosphate synthaseDomains of lifeProtein glycosylation reactionsStrong conservationCellular functionsG motifTerminal tailPrenyltransferase activityFirst enzymeCis-prenyltransferaseBacterial enzymesIsoprene unitsSubunitsLarge familyNgBREnzyme activityG sequencesEnzymeDolichyl phosphateMotifSynthaseEukaryotesOrthologsArchaea
2016
NgBR is essential for endothelial cell glycosylation and vascular development
Park EJ, Grabińska K, Guan Z, Sessa WC. NgBR is essential for endothelial cell glycosylation and vascular development. EMBO Reports 2016, 17: 167-177. PMID: 26755743, PMCID: PMC5290814, DOI: 10.15252/embr.201540789.Peer-Reviewed Original ResearchConceptsVascular developmentCis-prenyltransferase activityEmbryonic lethalityKnockout embryosProtein glycosylationTransmembrane proteinDefective glycosylationCell glycosylationEndothelial cellsDevelopment defectsKnockout resultsNgBRDolichol phosphateVE-cadherinGlycosylationYolk sacProteinEndothelial proteinsCellsIntegrated roleEmbryogenesisSubunitsEmbryosApoptosisEnd products
2014
Mutation of Nogo-B Receptor, a Subunit of cis-Prenyltransferase, Causes a Congenital Disorder of Glycosylation
Park EJ, Grabińska K, Guan Z, Stránecký V, Hartmannová H, Hodaňová K, Barešová V, Sovová J, Jozsef L, Ondrušková N, Hansíková H, Honzík T, Zeman J, Hůlková H, Wen R, Kmoch S, Sessa WC. Mutation of Nogo-B Receptor, a Subunit of cis-Prenyltransferase, Causes a Congenital Disorder of Glycosylation. Cell Metabolism 2014, 20: 448-457. PMID: 25066056, PMCID: PMC4161961, DOI: 10.1016/j.cmet.2014.06.016.Peer-Reviewed Original ResearchConceptsProtein glycosylationCis-prenyltransferaseGPI anchor biosynthesisDolichol synthesisSynthesis of dolicholO-mannosylationAnchor biosynthesisFirst enzymeGenetic basisC-terminusCongenital disorderFunction mutationsGlycosylationEssential roleEnhanced accumulationMutationsYeastNgBRSubunitsDolicholFibroblastsBiosynthesisTerminusFree cholesterolProtein