2024
Calcium flow at ER-TGN contact sites facilitates secretory cargo export
Ramazanov B, Parchure A, Di Martino R, Kumar A, Chung M, Kim Y, Griesbeck O, Schwartz M, Luini A, von Blume J. Calcium flow at ER-TGN contact sites facilitates secretory cargo export. Molecular Biology Of The Cell 2024, 35: ar50. PMID: 38294859, PMCID: PMC11064664, DOI: 10.1091/mbc.e23-03-0099.Peer-Reviewed Original Research
2023
Sorting secretory proteins
Parchure A, von Blume J. Sorting secretory proteins. ELife 2023, 12: e93490. PMID: 37997893, PMCID: PMC10672786, DOI: 10.7554/elife.93490.Peer-Reviewed Original Research
2022
Liquid–liquid phase separation facilitates the biogenesis of secretory storage granules
Parchure A, Tian M, Stalder D, Boyer C, Bearrows S, Rohli K, Zhang J, Rivera-Molina F, Ramazanov B, Mahata S, Wang Y, Stephens S, Gershlick D, von Blume J. Liquid–liquid phase separation facilitates the biogenesis of secretory storage granules. Journal Of Cell Biology 2022, 221: e202206132. PMID: 36173346, PMCID: PMC9526250, DOI: 10.1083/jcb.202206132.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkLiquid-liquid phase separationSecretory granulesClient moleculesSecretory storage granulesΒ-cellsMembrane traffickingCargo receptorsPlasma membranePancreatic β-cellsProcessing enzymesCell typesStorage granulesChromogranin proteinsBiogenesisAcidic pHTraffickingGranulesProteinEnzyme
2021
Cargo sorting at the trans-Golgi network at a glance
Ford C, Parchure A, von Blume J, Burd CG. Cargo sorting at the trans-Golgi network at a glance. Journal Of Cell Science 2021, 134 PMID: 34870705, PMCID: PMC8714066, DOI: 10.1242/jcs.259110.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkDistinct export pathwaysClathrin-coated vesiclesTrafficking of glycoproteinsMechanism of proteinEndo-lysosomal organellesAccompanying posterGlance articleResident proteinsExport pathwayGolgi functionTrans-GolgiDifferent organellesGolgi cisternaeKey molecular featuresTrans cisternaeMembrane sacsFinal compartmentGolgiCell surfaceDistinct repertoireCell scienceTransport carriersProteinOrganelles
2015
Oligomerization and endocytosis of Hedgehog is necessary for its efficient exovesicular secretion
Parchure A, Vyas N, Ferguson C, Parton R, Mayor S. Oligomerization and endocytosis of Hedgehog is necessary for its efficient exovesicular secretion. Molecular Biology Of The Cell 2015, 26: 4700-4717. PMID: 26490120, PMCID: PMC4678025, DOI: 10.1091/mbc.e15-09-0671.Peer-Reviewed Original ResearchConceptsLong-range signalingMultivesicular bodiesEndocytic deliveryDrosophila wing imaginal discWing imaginal discsESCRT proteinsLipidated proteinsSecreted morphogenImaginal discsNanoscale organizationExovesiclesHedgehogSignalingProteinOligomerizationHhDependent processesESCRTSelective effectTurn actMorphogensEndocytosisAqueous milieuSecretionComplexes