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
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
The isoprenoid biosynthetic pathway in Saccharomyces cerevisiae is affected in a maf1-1 mutant with altered tRNA synthesis
Kamińska J, Grabińska K, Kwapisz M, Sikora J, Smagowicz W, Palamarczyk G, Żołądek T, Boguta M. The isoprenoid biosynthetic pathway in Saccharomyces cerevisiae is affected in a maf1-1 mutant with altered tRNA synthesis. FEMS Yeast Research 2002, 2: 31-37. PMID: 12702319, DOI: 10.1111/j.1567-1364.2002.tb00066.x.Peer-Reviewed Original ResearchConceptsIsoprenoid pathwayIsoprenoid biosynthetic pathwayCellular tRNA levelsTRNA synthesisTRNA biosynthesisTRNA levelsSaccharomyces cerevisiaeBiosynthetic pathwayComplex regulationIsopentenyltransferaseProtein levelsMutantsErgosterol contentBiosynthesisPathwayIsopentenylationCerevisiaeSaccharomycesYeastTranscriptsRegulationExpressionDirect effectCells