Featured Publications
Motion of VAPB molecules reveals ER–mitochondria contact site subdomains
Obara C, Nixon-Abell J, Moore A, Riccio F, Hoffman D, Shtengel G, Xu C, Schaefer K, Pasolli H, Masson J, Hess H, Calderon C, Blackstone C, Lippincott-Schwartz J. Motion of VAPB molecules reveals ER–mitochondria contact site subdomains. Nature 2024, 626: 169-176. PMID: 38267577, PMCID: PMC10830423, DOI: 10.1038/s41586-023-06956-y.Peer-Reviewed Original ResearchConceptsContact sitesExchange of signaling moleculesInterorganelle communicationOrganelle tetheringEukaryotic cellsSingle-molecule imagingCellular physiologyThree-dimensional electron microscopyMembrane curvatureSignaling moleculesExchange of moleculesDynamic subdomainsNanoscale organizationProtein BMetabolic needsSubdomainsCellsSitesMutationsMoleculesRemodelingSites1,2HomeostasisCommunication hubRegulation
2024
Volume microscopic analysis of membrane contact sites in mouse kidney renal proximal tubule epithelial cells
Pandya R, Pang S, Lackner E, Reyna-Neyra A, Li W, Sy K, Burdyniuk M, Weisz O, Xu C, Caplan M. Volume microscopic analysis of membrane contact sites in mouse kidney renal proximal tubule epithelial cells. Physiology 2024, 39: 1086. DOI: 10.1152/physiol.2024.39.s1.1086.Peer-Reviewed Original ResearchMembrane contact sitesProximal tubule epithelial cellsTubule epithelial cellsEndoplasmic reticulumEpithelial cellsContact sitesPlasma membraneER volumeRenal proximal tubule epithelial cellsFunction of membrane contact sitesVolume of endoplasmic reticulumProximal tubule cellsInter-organelle communicationBasal-lateral surfacesRenal epithelial cellsAdvanced imaging techniquesMedian volumeTubule cellsMale miceCell plasma membraneRenal cortexScanning electron microscopyFIB-SEMMouse kidneySmooth ER
2019
Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III
Chang C, Weigel A, Ioannou M, Pasolli H, Xu C, Peale D, Shtengel G, Freeman M, Hess H, Blackstone C, Lippincott-Schwartz J. Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III. Journal Of Cell Biology 2019, 218: 2583-2599. PMID: 31227594, PMCID: PMC6683741, DOI: 10.1083/jcb.201902061.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid MotifsATP Binding Cassette Transporter, Subfamily D, Member 1Biological TransportEndosomal Sorting Complexes Required for TransportFatty AcidsHeLa CellsHumansHydrolysisLauric AcidsLipid DropletsModels, BiologicalMutant ProteinsOncogene ProteinsPeroxisomesSpastinConceptsFA traffickingLipid dropletsESCRT-III componentsNeutral lipid storage organellesLipid storage organellesFatty acid traffickingAAA-ATPaseESCRT-IIIDual roleMIT domainFatty acidsStorage organellesContact sitesPathogenesis of diseaseFA metabolismTraffickingPeroxisomesSpastinIST1OrganellesCHMP1BInterrelated mechanismsLipid peroxidationContact formationATPase