2021
Calcium levels in the Golgi complex regulate clustering and apical sorting of GPI-APs in polarized epithelial cells
Lebreton S, Paladino S, Liu D, Nitti M, von Blume J, Pinton P, Zurzolo C. Calcium levels in the Golgi complex regulate clustering and apical sorting of GPI-APs in polarized epithelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2014709118. PMID: 34389665, PMCID: PMC8379914, DOI: 10.1073/pnas.2014709118.Peer-Reviewed Original ResearchConceptsApical sortingGPI-APsCholesterol-dependent clusteringGolgi-resident proteinsPlasma membrane organizationPolarized epithelial cellsEpithelial cellsDiverse vital functionsResident proteinsMolecular machinerySecretory cargoMembrane organizationGolgi eventUnexpected roleGolgi complexSpecific machineryGolgiBasolateral surfaceApical surfaceCab45SPCA1Vital functionsMachinerySortingProtein
2020
Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3
Pigoni M, Hsia H, Hartmann J, Rudan Njavro J, Shmueli MD, Müller SA, Güner G, Tüshaus J, Kuhn P, Kumar R, Gao P, Tran ML, Ramazanov B, Blank B, Hipgrave Ederveen A, Von Blume J, Mulle C, Gunnersen JM, Wuhrer M, Rammes G, Busche MA, Koeglsperger T, Lichtenthaler SF. Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3. The EMBO Journal 2020, 39: embj2019103457. PMID: 32567721, PMCID: PMC7396870, DOI: 10.15252/embj.2019103457.Peer-Reviewed Original ResearchConceptsPrimary neuronsCell surface localizationMolecular functionsKainate receptor subunit GluK2Trafficking factorsSecretory pathwayNovel functionHeterologous cellsMajor substrateSurface localizationProtein 6Alzheimer's diseaseCA1 pyramidal neuronsAcute hippocampal slicesProtease BACE1Kainate-evoked currentsGlycosylationGluK2/3Pyramidal neuronsGluK2Hippocampal slicesKainate receptorsPsychiatric disordersNervous systemPsychiatric diseases
2019
Lipid‐dependent coupling of secretory cargo sorting and trafficking at the trans‐Golgi network
von Blume J, Hausser A. Lipid‐dependent coupling of secretory cargo sorting and trafficking at the trans‐Golgi network. FEBS Letters 2019, 593: 2412-2427. PMID: 31344259, PMCID: PMC8048779, DOI: 10.1002/1873-3468.13552.Peer-Reviewed Original ResearchExternalized histone H4 orchestrates chronic inflammation by inducing lytic cell death
Silvestre-Roig C, Braster Q, Wichapong K, Lee EY, Teulon JM, Berrebeh N, Winter J, Adrover JM, Santos GS, Froese A, Lemnitzer P, Ortega-Gómez A, Chevre R, Marschner J, Schumski A, Winter C, Perez-Olivares L, Pan C, Paulin N, Schoufour T, Hartwig H, González-Ramos S, Kamp F, Megens RTA, Mowen KA, Gunzer M, Maegdefessel L, Hackeng T, Lutgens E, Daemen M, von Blume J, Anders HJ, Nikolaev VO, Pellequer JL, Weber C, Hidalgo A, Nicolaes GAF, Wong GCL, Soehnlein O. Externalized histone H4 orchestrates chronic inflammation by inducing lytic cell death. Nature 2019, 569: 236-240. PMID: 31043745, PMCID: PMC6716525, DOI: 10.1038/s41586-019-1167-6.Peer-Reviewed Original ResearchConceptsSmooth muscle cellsChronic inflammationDestabilization of plaquesGlobal medical burdenImportant pathophysiological contributorCell deathPerpetuation of inflammationChronic vascular diseaseNeutrophil extracellular trapsMajor underlying causeLytic cell deathPathophysiological contributorVascular diseaseMedical burdenExtracellular trapsMouse modelAtherosclerotic lesionsMolecular mediatorsInflammationTissue damageTherapeutic valueMuscle cellsUnderlying causeDeathHistone H4Signal peptide peptidase‐like 2c impairs vesicular transport and cleaves SNARE proteins
Papadopoulou A, Müller S, Mentrup T, Shmueli M, Niemeyer J, Haug‐Kröper M, von Blume J, Mayerhofer A, Feederle R, Schröder B, Lichtenthaler S, Fluhrer R. Signal peptide peptidase‐like 2c impairs vesicular transport and cleaves SNARE proteins. EMBO Reports 2019, 20: embr201846451. PMID: 30733281, PMCID: PMC6399617, DOI: 10.15252/embr.201846451.Peer-Reviewed Original ResearchMeSH KeywordsAcrosomeAnimalsAspartic Acid EndopeptidasesBiocatalysisDown-RegulationGlycomicsGlycoproteinsGlycosyltransferasesGolgi ApparatusHEK293 CellsHumansMaleMembrane ProteinsMice, Inbred C57BLModels, BiologicalProtein TransportProteolysisSNARE ProteinsSpermatidsSubcellular FractionsSubstrate SpecificityConceptsSNARE proteinsCandidate substratesVesicular transportProcess of vesicular traffickingImpaired vesicular transportIntramembrane aspartyl proteaseCleave SNARE proteinsGxGD-typeAcrosome formationB cell developmentCargo proteinsVesicular traffickingAspartyl proteaseProtease familyCellular processesProtein glycosylationSubcellular compartmentsEndoplasmic reticulumProteolytic processingBiological processesAlzheimer's diseasePhysiological functionsProteinDevelopment of pathologyProtease
2017
Cab45—Unraveling key features of a novel secretory cargo sorter at the trans-Golgi network
Blank B, von Blume J. Cab45—Unraveling key features of a novel secretory cargo sorter at the trans-Golgi network. European Journal Of Cell Biology 2017, 96: 383-390. PMID: 28372832, DOI: 10.1016/j.ejcb.2017.03.001.Peer-Reviewed Original ResearchConceptsMolecular functionsCargo moleculesCytoplasmic actin cytoskeletonSpecific cargo moleculesTransmembrane cargo receptorsTrans-Golgi networkMannose-6-phosphate receptorCargo receptorsGolgi networkActin cytoskeletonATPase SPCA1Secreted proteinsPlasma membraneSecretory proteinsExtracellular proteasesCab45Sorting mechanismSurface receptorsProteinExtracellular spaceSpecific carrierPossible roleFinal destinationSortingReceptors
2015
Julia von Blume: Sorting through the trans-Golgi
von Blume J, Sedwick C. Julia von Blume: Sorting through the trans-Golgi. Journal Of Cell Biology 2015, 208: 4-5. PMID: 25559180, PMCID: PMC4284231, DOI: 10.1083/jcb.2081pi.Peer-Reviewed Original Research
2014
Secretory cargo sorting at the trans-Golgi network
Kienzle C, von Blume J. Secretory cargo sorting at the trans-Golgi network. Trends In Cell Biology 2014, 24: 584-593. PMID: 24841758, DOI: 10.1016/j.tcb.2014.04.007.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkCytoplasmic actin cytoskeletonPlasma membrane deliverySubset of proteinsNovel sorting mechanismKey cellular eventsSecretory cargoActin cytoskeletonCellular eventsBinding proteinLysosomal hydrolasesSorting mechanismProteinNormal physiologySuccessful sortingRecent discoverySortingCab45CytoskeletonHydrolasesSPCA1ATPaseRegulationPhysiologyCargo
2013
Directing Traffic into the Future
Antonny B, Audhya J, l Bagnat M, von Blume J, Briggs JA, Giraudo C, Kaeser PS, Miller E, Reinisch K, Sbalzarini IF, Schuldiner M, Shen J, Takamori S, Verstreken P, Walther T. Directing Traffic into the Future. Developmental Cell 2013, 27: 480-484. PMID: 24482802, DOI: 10.1016/j.devcel.2013.11.017.Peer-Reviewed Original Research
2009
Actin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network
von Blume J, Duran JM, Forlanelli E, Alleaume AM, Egorov M, Polishchuk R, Molina H, Malhotra V. Actin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network. Journal Of Cell Biology 2009, 187: 1055-1069. PMID: 20026655, PMCID: PMC2806282, DOI: 10.1083/jcb.200908040.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkADF/cofilinActin-depolymerizing factorSecretory proteinsSecretory cargoCofilin knockdownMass spectrometry-based protein profilingMammalian tissue culture cellsGolgi-resident proteinsSorting of proteinsEndogenous secretory proteinsIntegral membrane proteinsSoluble secretory proteinsStable isotope labelingTissue culture cellsDrosophila melanogasterActin remodelingMammalian cellsMembrane proteinsGolgi membranesProtein profilingIsotope labelingCofilinCell surfaceAmino acids
2007
Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2
von Blume J, Knippschild U, Dequiedt F, Giamas G, Beck A, Auer A, Van Lint J, Adler G, Seufferlein T. Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2. The EMBO Journal 2007, 26: 4619-4633. PMID: 17962809, PMCID: PMC2080801, DOI: 10.1038/sj.emboj.7601891.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCasein Kinase 1 epsilonCasein Kinase IdeltaCell LineCell Line, TumorCell NucleusChlorocebus aethiopsCOS CellsDNA-Binding ProteinsGastrinsHeLa CellsHistone DeacetylasesHumansNuclear Receptor Subfamily 4, Group A, Member 1PhosphorylationProtein Kinase CProtein Kinase D2Protein KinasesReceptor, Cholecystokinin BReceptors, Cytoplasmic and NuclearReceptors, SteroidSerineTranscription FactorsConceptsProtein kinase D2Nuclear accumulationEfficient phosphorylationCritical post-translational modificationSerine/threonine kinaseZinc finger domainPost-translational modificationsSignal transduction pathwaysG protein-coupled receptorsHuman gastric cancer cellsExport machinerySubstrate targetingHDAC7 phosphorylationActivation loopNuclear substratesThreonine kinaseActive kinaseNuclear exportGastric cancer cellsSubcellular compartmentsTransduction pathwaysNuclear localizationPKD familyPKC etaPhosphorylation
2006
New Role for hPar-1 Kinases EMK and C-TAK1 in Regulating Localization and Activity of Class IIa Histone Deacetylases
Dequiedt F, Martin M, Von Blume J, Vertommen D, Lecomte E, Mari N, Heinen MF, Bachmann M, Twizere JC, Huang MC, Rider MH, Piwnica-Worms H, Seufferlein T, Kettmann R. New Role for hPar-1 Kinases EMK and C-TAK1 in Regulating Localization and Activity of Class IIa Histone Deacetylases. Molecular And Cellular Biology 2006, 26: 7086-7102. PMID: 16980613, PMCID: PMC1592903, DOI: 10.1128/mcb.00231-06.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsActive Transport, Cell NucleusAmino Acid SequenceAnimalsBinding SitesCell NucleusCells, CulturedChlorocebus aethiopsCOS CellsCytoplasmHeLa CellsHistone DeacetylasesHumansMolecular Sequence DataPhosphorylationPhosphoserineProtein Serine-Threonine KinasesProtein TransportSubstrate SpecificityConceptsMicrotubule affinity-regulating kinaseClass IIa HDACsN-terminal serine residueClass IIa histoneIIa HDACsC-TAK1IIa histoneSerine residuesMajor developmental programsMARK/ParVariety of kinasesHierarchical phosphorylationRepressive activityNuclear exportRepressive functionDevelopmental programSubcellular localizationNuclear exclusionConstitutive phosphorylationSophisticated regulationPhosphorylationKinaseSpecific signalsHDACsHistones