2021
Progressive myoclonus epilepsies—Residual unsolved cases have marked genetic heterogeneity including dolichol-dependent protein glycosylation pathway genes
Courage C, Oliver KL, Park EJ, Cameron JM, Grabińska KA, Muona M, Canafoglia L, Gambardella A, Said E, Afawi Z, Baykan B, Brandt C, di Bonaventura C, Chew HB, Criscuolo C, Dibbens LM, Castellotti B, Riguzzi P, Labate A, Filla A, Giallonardo AT, Berecki G, Jackson CB, Joensuu T, Damiano JA, Kivity S, Korczyn A, Palotie A, Striano P, Uccellini D, Giuliano L, Andermann E, Scheffer IE, Michelucci R, Bahlo M, Franceschetti S, Sessa WC, Berkovic SF, Lehesjoki AE. Progressive myoclonus epilepsies—Residual unsolved cases have marked genetic heterogeneity including dolichol-dependent protein glycosylation pathway genes. American Journal Of Human Genetics 2021, 108: 722-738. PMID: 33798445, PMCID: PMC8059372, DOI: 10.1016/j.ajhg.2021.03.013.Peer-Reviewed Original ResearchConceptsPME genesProgressive myoclonus epilepsyWhole-exome sequencingPrevious genetic analysisGroup of genesVariety of proteinsPrevious disease associationsUnrelated individualsCopy number changesProtein glycosylationPathway genesEndosomal functionGenetic analysisDisease-causing variantsGenesLikely disease-causing variantsAdditional family membersGenetic heterogeneityHeterogeneous rare diseasesUnsolved casesDisease associationsNovel causeMyoclonus epilepsyHeterozygous variantsHomozygous variant
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
Long-Chain Polyprenols Promote Spore Wall Formation in Saccharomyces cerevisiae
Hoffmann R, Grabińska K, Guan Z, Sessa WC, Neiman AM. Long-Chain Polyprenols Promote Spore Wall Formation in Saccharomyces cerevisiae. Genetics 2017, 207: 1371-1386. PMID: 28978675, PMCID: PMC5714454, DOI: 10.1534/genetics.117.300322.Peer-Reviewed Original ResearchConceptsLong-chain polyprenolsSpore wallSynthesis of chitinSpore wall layerHaploid genomeCellular processesProtein glycosylationPrenyltransferase activitySporulating cellsWall formationDityrosine layerIsoprenoid lipidsChitin synthaseEndoplasmic reticulumVegetative cellsSRT1Lipid dropletsDividing cellsEssential precursorPrimary enzymeImportant functionsSaccharomycesPolyprenolsDolicholSugar carrier
2016
cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases*
Grabińska K, Park EJ, Sessa WC. cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases*. Journal Of Biological Chemistry 2016, 291: 18582-18590. PMID: 27402831, PMCID: PMC5000101, DOI: 10.1074/jbc.r116.739490.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsUndecaprenyl diphosphate synthaseIsopentenyl diphosphateDomains of lifeConsecutive condensation reactionsPlant orthologsHeteromeric enzymeCis-PrenyltransferasesDiphosphate synthaseProtein glycosylationPolyprenyl diphosphateBacterial enzymesHuman diseasesMode of actionLarge familyOrthologsEnzymeRubber synthesisSubunitsNew insightsCarbon skeletonStructural componentsDiphosphateMammalsFungalGlycosylationNgBR 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
2005
Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.
Kamińska J, Kwapisz M, Grabińska K, Orłowski J, Boguta M, Palamarczyk G, Zoładek T. Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae. Acta Biochimica Polonica 2005, 52: 207-20. PMID: 15827618, DOI: 10.18388/abp.2005_3510.Peer-Reviewed Original ResearchConceptsCell wall integrityIsoprenoid pathwayWall integrityPlasma membraneRsp5 ubiquitin-protein ligaseCell wallCell wall organizationRsp5 ubiquitin ligaseUbiquitin-protein ligaseCell wall structureWild-type strainNorthern blot analysisWall organizationProtein glycosylationDimethylallyl diphosphateType strainUbiquitin ligaseIsopentenyl diphosphateS. cerevisiaeCytosolic distributionErgosterol biosynthesisKey enzymeRegulatory roleChitin levelsMolecular level
2002
Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase
Grabińska K, Palamarczyk G. Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Research 2002, 2: 259-265. DOI: 10.1111/j.1567-1364.2002.tb00093.x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsDolichol biosynthesisMevalonate pathwayYeast Saccharomyces cerevisiaeTranscription of genesAAA ATPase familyNon-sterol derivativesEffects of overexpressionATPase familyNon-sterol compoundsProtein glycosylationSaccharomyces cerevisiaeFirst enzymeIsoprenoid lipidsRegulatory enzymeRegulatory roleEffects of FPPBiosynthesisFarnesylCoA reductaseMevalonic acidPathwayEnzymeSynthaseFPPPresent reviewDolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase
Grabińska K, Palamarczyk G. Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Research 2002, 2: 259-265. PMID: 12702274, DOI: 10.1016/s1567-1356(02)00110-1.Peer-Reviewed Original ResearchConceptsFarnesyl diphosphateDolichol biosynthesisMevalonate pathwayOverexpression of farnesyl diphosphate synthaseYeast Saccharomyces cerevisiaeAAA ATPase familyFarnesyl diphosphate synthaseDerivatives of mevalonic acidDiphosphate synthaseProtein glycosylationATPase familyIsoprenoid lipidsRegulatory enzymeMevalonic acidMevalonateRegulatory roleBiosynthesisDolicholYeastPathwayProteinEnzymeYta7FarnesylationTranscription