2021
De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus
Galosi S, Edani BH, Martinelli S, Hansikova H, Eklund EA, Caputi C, Masuelli L, Corsten-Janssen N, Srour M, Oegema R, Bosch DGM, Ellis CA, Amlie-Wolf L, Accogli A, Atallah I, Averdunk L, Barañano KW, Bei R, Bagnasco I, Brusco A, Demarest S, Alaix AS, Di Bonaventura C, Distelmaier F, Elmslie F, Gan-Or Z, Good JM, Gripp K, Kamsteeg EJ, Macnamara E, Marcelis C, Mercier N, Peeden J, Pizzi S, Pannone L, Shinawi M, Toro C, Verbeek NE, Venkateswaran S, Wheeler PG, Zdrazilova L, Zhang R, Zorzi G, Guerrini R, Sessa WC, Lefeber DJ, Tartaglia M, Hamdan FF, Grabińska KA, Leuzzi V. De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus. Brain 2021, 145: 208-223. PMID: 34382076, PMCID: PMC8967098, DOI: 10.1093/brain/awab299.Peer-Reviewed Original ResearchConceptsRetinitis pigmentosaNeurodegenerative disordersMovement disordersDe novo pathogenic variantsHypokinetic movement disordersCongenital disorderLong-term outcomesNeurodevelopmental disordersNovo pathogenic variantsNeuronal ceroid lipofuscinosisProgressive myoclonus epilepsyDisease courseNeurological declineClinical featuresProgressive encephalopathyPsychiatric disturbancesMyelinated fibersLarge cohortCortical tremorCognitive deteriorationDisease-causing variantsEndosomal-lysosomal pathwayAutosomal recessive formPathogenic variantsAltered lysosomesProgressive 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
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
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
2010
Molecular characterization of the cis-prenyltransferase of Giardia lamblia
Grabińska K, Cui J, Chatterjee A, Guan Z, Raetz C, Robbins P, Samuelson J. Molecular characterization of the cis-prenyltransferase of Giardia lamblia. Glycobiology 2010, 20: 824-832. PMID: 20308470, PMCID: PMC2900897, DOI: 10.1093/glycob/cwq036.Peer-Reviewed Original ResearchConceptsIsoprene unitsDouble deletion mutantGPI anchor synthesisMost eukaryotesHigher eukaryotesAnchor synthesisN-glycosylationGlycosylphosphatidylinositol (GPI) anchorCis-prenyltransferaseKinase activityPolyprenyl pyrophosphateBacterial enzymesDolichol kinase activityDolichol kinaseMolecular characterizationImportant enzymeN-glycansEukaryotesProtistsPolyprenol lipidsNormal growthPyrophosphate linkageEnzymeGiardia lambliaDolichol
2005
Functional relationships between the Saccharomyces cerevisiae cis-prenyltransferases required for dolichol biosynthesis.
Grabińska K, Sosińska G, Orłowski J, Swiezewska E, Berges T, Karst F, Palamarczyk G. Functional relationships between the Saccharomyces cerevisiae cis-prenyltransferases required for dolichol biosynthesis. Acta Biochimica Polonica 2005, 52: 221-32. PMID: 15827619, DOI: 10.18388/abp.2005_3511.Peer-Reviewed Original ResearchConceptsEnzymatic activityCis-prenyltransferase activityLong-chain dolicholsYeast SaccharomycesShorter speciesRER2Dolichol biosynthesisLevels of mRNADiphosphate formationIsoprene unitsSRT1SaccharomycesOverexpressionDolichol contentGenesPreferential synthesisProteinFunctional relationshipMRNADPM1TranscriptionBiosynthesisFarnesylSpecies
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
1997
Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression
Szkopińska A, Grabińska K, Delourme D, Karst F, Rytka J, Palamarczyk G. Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression. Journal Of Lipid Research 1997, 38: 962-968. PMID: 9186913, DOI: 10.1016/s0022-2275(20)37220-5.Peer-Reviewed Original ResearchConceptsWild-type yeastType yeastSaccharomyces cerevisiaeYeast Saccharomyces cerevisiaeEffects of farnesylSynthesis of dolicholSame genetic backgroundHand overexpressionErg mutantsFPP synthaseSqualene synthase activitySynthesis of polyprenolsExogenous FPPMevalonate pathwayMutantsGenetic backgroundYeastOverexpressionSynthase overexpressionSynthase activityCerevisiaeFarnesylGenesSynthasePolyprenols