2021
Sending out molecules from the TGN
Ramazanov BR, Tran ML, von Blume J. Sending out molecules from the TGN. Current Opinion In Cell Biology 2021, 71: 55-62. PMID: 33706234, PMCID: PMC8328904, DOI: 10.1016/j.ceb.2021.02.005.Peer-Reviewed Original ResearchMeSH KeywordsCell MembraneEndoplasmic ReticulumMembrane ProteinsProtein TransportTrans-Golgi NetworkConceptsTrans-Golgi networkEndoplasmic reticulum contact sitesCell-cell communicationExtracellular matrix proteinsMembrane traffickingCargo proteinsCargo sortingTGN structureTransmembrane proteinPlasma membraneContact sitesExciting linkSoluble proteinMatrix proteinsSorting mechanismProteinTransport carriersMajor open questionsSortingMembraneNovel typeTraffickingMachineryOrganismsVesicles
2019
Signal 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
2014
JAGN1 deficiency causes aberrant myeloid cell homeostasis and congenital neutropenia
Boztug K, Järvinen PM, Salzer E, Racek T, Mönch S, Garncarz W, Gertz EM, Schäffer AA, Antonopoulos A, Haslam SM, Schieck L, Puchałka J, Diestelhorst J, Appaswamy G, Lescoeur B, Giambruno R, Bigenzahn JW, Elling U, Pfeifer D, Conde CD, Albert MH, Welte K, Brandes G, Sherkat R, van der Werff ten Bosch J, Rezaei N, Etzioni A, Bellanné-Chantelot C, Superti-Furga G, Penninger JM, Bennett KL, von Blume J, Dell A, Donadieu J, Klein C. JAGN1 deficiency causes aberrant myeloid cell homeostasis and congenital neutropenia. Nature Genetics 2014, 46: 1021-1027. PMID: 25129144, PMCID: PMC4829076, DOI: 10.1038/ng.3069.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAdultApoptosisCell DifferentiationCell SurvivalChildChild, PreschoolCongenital Bone Marrow Failure SyndromesFemaleGlycosylationHomeostasisHumansInfantInfant, NewbornMaleMembrane ProteinsMutationMyeloid CellsNeutropeniaNeutrophilsReceptors, Granulocyte Colony-Stimulating FactorSignal TransductionYoung Adult
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