2020
Palmitoylated Proteins in Plasmodium falciparum‐Infected Erythrocytes: Investigation with Click Chemistry and Metabolic Labeling
Kilian N, Zhang Y, LaMonica L, Hooker G, Toomre D, Mamoun CB, Ernst AM. Palmitoylated Proteins in Plasmodium falciparum‐Infected Erythrocytes: Investigation with Click Chemistry and Metabolic Labeling. BioEssays 2020, 42: e1900145. PMID: 32342554, DOI: 10.1002/bies.201900145.Peer-Reviewed Original ResearchConceptsMetabolic labelingHuman malaria parasite Plasmodium falciparumProtein S-palmitoylationImportant post-translational modificationMalaria parasite Plasmodium falciparumComplex cell biologyPost-translational modificationsParasite Plasmodium falciparumTime-consuming generationAsexual developmental stagesPalmitoylated proteinsS-palmitoylationCell biologyP. falciparumTransgenic parasitesExtent of labelingDevelopmental stagesMicroscopy approachSingle-molecule switchingPlasmodium falciparum-infected erythrocytesFalciparum-infected erythrocytesPlasmodium falciparumFalciparumLabelingMicroscopic examination
2018
S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi
Ernst AM, Syed SA, Zaki O, Bottanelli F, Zheng H, Hacke M, Xi Z, Rivera-Molina F, Graham M, Rebane AA, Björkholm P, Baddeley D, Toomre D, Pincet F, Rothman JE. S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi. Developmental Cell 2018, 47: 479-493.e7. PMID: 30458139, PMCID: PMC6251505, DOI: 10.1016/j.devcel.2018.10.024.Peer-Reviewed Original ResearchConceptsS-palmitoylationAnterograde cargoAnterograde signalMembrane cargoCargo selectionTransmembrane domainMembrane proteinsGolgi membranesGolgiSpecific signalsMembrane interfaceModel systemCargoProteinRate of transportAnterograde transportVesiclesCisternaeCurved regionsMembraneTransportRegionSignalsDomainFluorescence
2012
Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases
Marin EP, Derakhshan B, Lam TT, Davalos A, Sessa WC. Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases. Circulation Research 2012, 110: 1336-1344. PMID: 22496122, PMCID: PMC3428238, DOI: 10.1161/circresaha.112.269514.Peer-Reviewed Original ResearchMeSH KeywordsAcetyltransferasesAcyltransferasesAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsEndothelial CellsHEK293 CellsHuman Umbilical Vein Endothelial CellsHumansLipoylationMolecular Sequence DataPlatelet Endothelial Cell Adhesion Molecule-1ProteomicsRNA, Small InterferingSubstrate SpecificitySuperoxide DismutaseSuperoxide Dismutase-1ConceptsProtein acyl transferasesAcyl-biotinyl exchangeProtein S-palmitoylationPlatelet endothelial cell adhesion molecule-1Posttranslational lipid modificationRole of palmitoylationEndothelial cell adhesion molecule-1Acyl transferaseEndothelial cell biologyPalmitoyl proteinsS-palmitoylationPosttranslational attachmentProtein localizationCysteine side chainsCell biologyNuclear localizationPalmitoylationLipid modificationEC biologyThioester bondCell adhesion molecule-1Superoxide dismutase 1Functional roleCell surfacePotential substrates
2006
Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase
Fernández-Hernando C, Fukata M, Bernatchez PN, Fukata Y, Lin MI, Bredt DS, Sessa WC. Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase. Journal Of Cell Biology 2006, 174: 369-377. PMID: 16864653, PMCID: PMC2064233, DOI: 10.1083/jcb.200601051.Peer-Reviewed Original ResearchConceptsHuman endothelial cellsComplementary DNAPalmitoylation-deficient mutantHuman embryonic kidney 293 cellsEmbryonic kidney 293 cellsEndothelial nitric oxide synthaseEndothelial cellsKidney 293 cellsDHHC enzymesN-myristoylationS-palmitoylationNew GolgiSubcellular localizationCDNA clonesPlasma membraneLipid modificationCytoplasmic aspectENOS localizationGolgi apparatusRegulatory roleENOS palmitoylationPalmitoyl transferaseGolgiNitric oxide synthaseAcyl transferase
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