2025
ER tubular body: an ER-derived compartment for redirecting autophagy to secretory functions
Song M, Sim H, Noh S, Malhotra V, Lee M. ER tubular body: an ER-derived compartment for redirecting autophagy to secretory functions. Autophagy 2025, ahead-of-print: 1-3. PMID: 40390263, DOI: 10.1080/15548627.2025.2508935.Peer-Reviewed Original ResearchPositive-strand RNA virusesConditions of cellular stressFormation of membrane compartmentsER-derived compartmentSecretion of proteinsCell surface traffickingReticulophagy receptorER remodelingVesicle traffickingProtein homeostasisMembrane compartmentsEndoplasmic reticulumActivation of UCPRNA virusesTransmembrane proteinsCellular stressProtein secretionTrafficking defectTubulovesicular networkPotential therapeutic strategyViral pathogenesisProteinViral replicationSecretory functionTubular bodyCRISPR-Cas13d Functional Transcriptomics Reveals Widespread Isoform-Selective Cancer Dependencies on LncRNAs
Morelli E, Aktas Samur A, Maisano D, Gao C, Favasuli V, Papaioannou D, De Nola G, Henninger J, Liu N, Turi M, Folino P, Vreux L, Cumerlato M, Chen L, Aifantis I, Fulciniti M, Anderson K, Lytton-Jean A, Gulla A, Young R, Samur M, Munshi N. CRISPR-Cas13d Functional Transcriptomics Reveals Widespread Isoform-Selective Cancer Dependencies on LncRNAs. Blood 2025 PMID: 40403231, DOI: 10.1182/blood.2025028746.Peer-Reviewed Original ResearchCRISPR-Cas13dMultiple myelomaTE-lncRNAsIsoform-specific functionsDiverse cancer cell linesMM patientsCancer cell linesCellular proteostasisSubcellular localizationTumor cellsClinical dataCancer transcriptomeCytosolic isoformEndoplasmic reticulumFunctional transcriptomeHeat shock proteinsCancer dependenciesMM-specificClinical relevanceAnimal modelsLong noncoding RNAsLncRNA transcriptomeTherapeutic potentialCharacterize hundredsTranscriptomeCompartmentalization of the Endoplasmic Reticulum in Mouse Kidney Proximal Tubule Epithelial Cells
Reyna-Neyra A, Pandya R, Lackner E, Pang S, Li W, Xu C, Zugates C, Burdyniuk M, Pandya V, Weisz O, Caplan M. Compartmentalization of the Endoplasmic Reticulum in Mouse Kidney Proximal Tubule Epithelial Cells. Physiology 2025, 40: 1280. DOI: 10.1152/physiol.2025.40.s1.1280.Peer-Reviewed Original ResearchPT cellsProximal tubulesEndoplasmic reticulumER structureKidney proximal tubule epithelial cellsProximal tubule epithelial cellsER proteinsRenal proximal tubulesProximal tubule cellsKidney proximal tubulesTubule epithelial cellsBasolateral plasma membraneOuter membrane proteinsCalcium ATPaseTubule cellsSolute reabsorptionCalcium ion storageMouse kidney tissuesK-ATPaseMean volumeEpithelial cellsER lumenCLIMP-63ER volumeMouse kidneyLipid Dynamics at Membrane Contact Sites
Reinisch K, De Camilli P, Melia T. Lipid Dynamics at Membrane Contact Sites. Annual Review Of Biochemistry 2025, 94: 479-502. PMID: 40067957, DOI: 10.1146/annurev-biochem-083024-122821.Peer-Reviewed Original ResearchConceptsContact sitesOrganelle contact sitesMembrane contact sitesIntegral membrane proteinsLipid transfer proteinsVesicular traffickingEndoplasmic reticulumLipid transferMembrane proteinsLipid movementOrganellesLipid transportTransfer proteinCellular membranesProteinBilayer asymmetryLipid dynamicsShedding new lightLipidMembranePhysiological mechanismsEukaryotesSitesReticulumTraffickingThe pathways of secretory cargo export at the endoplasmic reticulum
Malhotra V. The pathways of secretory cargo export at the endoplasmic reticulum. Nature Communications 2025, 16: 2138. PMID: 40032897, PMCID: PMC11876584, DOI: 10.1038/s41467-025-57408-2.Peer-Reviewed Original Research
2024
DNA-Assisted Assays for Studying Lipid Transfer Between Membranes
Wang Y, Shi Q, Yang Q, Yang Y, Bian X. DNA-Assisted Assays for Studying Lipid Transfer Between Membranes. Methods In Molecular Biology 2024, 2888: 221-236. PMID: 39699734, DOI: 10.1007/978-1-0716-4318-1_15.Peer-Reviewed Original ResearchConceptsSynaptotagmin-like mitochondrial lipid-binding proteinLipid transfer assaysFluorescence resonance energy transferEndoplasmic reticulumLipid transferPlasma membraneLipid-binding proteinsLipid transfer proteinsTransfer assayE-SytsExtended-synaptotagminsResonance energy transferLipid homeostasisReleased lipidsTransfer proteinProteinAssayMembraneLipidTransfer signalsReticulumHomeostasisEnergy transferEctopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation
Falahati H, Wu Y, Fang M, De Camilli P. Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation. Current Biology 2024, 35: 265-276.e4. PMID: 39626668, PMCID: PMC11753949, DOI: 10.1016/j.cub.2024.11.010.Peer-Reviewed Original ResearchEndoplasmic reticulumSpine apparatusActin bundlesEndomembrane networkER sheetsConserved regionProtein synaptopodinCisternal organelleNon-neuronal cellsER cisternsOrganellesSynaptopodinProteinNeuronal dendritesNeuronal spinesAxon initial segmentFindings shed lightBiogenesisActinProtein matrixNarrow lumenReticulumMammalsInitial segmentMechanismDominant negative variants in ITPR3 impair T cell Ca2+ dynamics causing combined immunodeficiency
Blanco E, Camps C, Bahal S, Kerai M, Ferla M, Rochussen A, Handel A, Golwala Z, Goncalves H, Kricke S, Klein F, Zhang F, Zinghirino F, Evans G, Keane T, Lizot S, Kusters M, Iro M, Patel S, Morris E, Burns S, Radcliffe R, Vasudevan P, Price A, Gillham O, Valdebenito G, Stewart G, Worth A, Adams S, Duchen M, André I, Adams D, Santili G, Gilmour K, Holländer G, Davies E, Taylor J, Griffiths G, Thrasher A, Dhalla F, Kreins A. Dominant negative variants in ITPR3 impair T cell Ca2+ dynamics causing combined immunodeficiency. Journal Of Experimental Medicine 2024, 222: e20220979. PMID: 39560673, PMCID: PMC11577440, DOI: 10.1084/jem.20220979.Peer-Reviewed Original ResearchConceptsStore-operated Ca2+ entryRelease of ER Ca2+Combined immunodeficiencyEndoplasmic reticulumDe novo missense variantDepletion of ER Ca2+ storesER Ca2+T cellsER Ca2+ storesDominant negative variantTriggers store-operated Ca2+ entryThymic T cell developmentInositol 1,4,5-trisphosphate receptorT cell developmentT-cell lymphopeniaT-cell immunodeficiencyCa2+ storesCa2+ entryCa2+ channelsMissense variantsT cell signalingPeripheral T cellsCa2+ homeostasisNegative variantsCa2+ dynamicsRedox regulation, protein S-nitrosylation, and synapse loss in Alzheimer’s and related dementias
Oh C, Nakamura T, Zhang X, Lipton S. Redox regulation, protein S-nitrosylation, and synapse loss in Alzheimer’s and related dementias. Neuron 2024, 112: 3823-3850. PMID: 39515322, PMCID: PMC11624102, DOI: 10.1016/j.neuron.2024.10.013.Peer-Reviewed Original ResearchProtein S-nitrosylationS-nitrosylationEndoplasmic reticulumRedox-mediated posttranslational modificationDiseases associated with protein aggregationProtein aggregationSynapse lossModulating protein activityNetwork of proteinsMultiple neurodegenerative disordersUbiquitin-proteasome systemS-nitrosylation reactionPosttranslational modificationsMitochondrial metabolismExcessive nitrosative stressEnzymatic machineryRedox regulationProtein activityProtein networkDysfunction pathwayMicroglial phagocytosisSingle proteinsBioenergetic compromiseReview recent findingsProteinBeyond glucose: The crucial role of redox signaling in β-cell metabolic adaptation
Holendová B, Šalovská B, Benáková Š, Plecitá-Hlavatá L. Beyond glucose: The crucial role of redox signaling in β-cell metabolic adaptation. Metabolism 2024, 161: 156027. PMID: 39260557, DOI: 10.1016/j.metabol.2024.156027.Peer-Reviewed Original ResearchPost-translational modificationsReactive oxygen speciesEndoplasmic reticulumTricarboxylic acidRedox signalingPancreatic B-cellsGlucose stimulationModification of proteinsB-cell metabolismRedox signaling pathwaysReversible cysteine oxidationIncreased ROS levelsProduction of reactive oxygen speciesB cell functionInsulin secretionB cellsProtein functionProtein processingCysteine thiol modificationsGlucose-induced increaseOxidative phosphorylationPyruvate metabolismProtein activityRegulatory mechanismsMetabolic pathwaysPublisher Correction: Intestinal Nogo-B reduces GLP1 levels by binding to proglucagon on the endoplasmic reticulum to inhibit PCSK1 cleavage
Gong K, Xue C, Feng Z, Pan R, Wang M, Chen S, Chen Y, Guan Y, Dai L, Zhang S, Jiang L, Li L, Wang B, Yin Z, Ma L, Iwakiri Y, Tang J, Liao C, Chen H, Duan Y. Publisher Correction: Intestinal Nogo-B reduces GLP1 levels by binding to proglucagon on the endoplasmic reticulum to inhibit PCSK1 cleavage. Nature Communications 2024, 15: 7902. PMID: 39256382, PMCID: PMC11387603, DOI: 10.1038/s41467-024-52287-5.Peer-Reviewed Original ResearchIntestinal Nogo-B reduces GLP1 levels by binding to proglucagon on the endoplasmic reticulum to inhibit PCSK1 cleavage
Gong K, Xue C, Feng Z, Pan R, Wang M, Chen S, Chen Y, Guan Y, Dai L, Zhang S, Jiang L, Li L, Wang B, Yin Z, Ma L, Iwakiri Y, Tang J, Liao C, Chen H, Duan Y. Intestinal Nogo-B reduces GLP1 levels by binding to proglucagon on the endoplasmic reticulum to inhibit PCSK1 cleavage. Nature Communications 2024, 15: 6845. PMID: 39122737, PMCID: PMC11315690, DOI: 10.1038/s41467-024-51352-3.Peer-Reviewed Original ResearchConceptsEnteroendocrine cellsEndoplasmic reticulum (ER)-resident proteinGlucagon-like peptide 1Nogo-BEndoplasmic reticulumStimulate insulin secretionPotential therapeutic targetProglucagonGlucagon-like peptide 1 receptorInhibit glucagon secretionRegulatory processesIntestinal tractProglucagon fragmentInsulin secretionCleavageNogo-B knockoutTherapeutic targetPancreatic cellsPeptide 1Glucagon secretionCellsReticulonGolgiReticulon 4BInsulin resistanceTailored assemblies of COPII proteins in secretion
Malhotra V. Tailored assemblies of COPII proteins in secretion. Journal Of Cell Biology 2024, 223: e202404013. PMID: 38958655, PMCID: PMC11222725, DOI: 10.1083/jcb.202404013.Peer-Reviewed Original ResearchARID1A in Gynecologic Precancers and Cancers
Morgan J, Jaferi N, Shonibare Z, Huang G. ARID1A in Gynecologic Precancers and Cancers. Reproductive Sciences 2024, 31: 2150-2162. PMID: 38740655, DOI: 10.1007/s43032-024-01585-w.Peer-Reviewed Original ResearchARID1A alterationsGynecologic cancerTumor suppressor ARID1AResponse to chemotherapeutic agentsFrequency of genetic alterationsLoss-of-function mutationsSWI/SNF complex subunitsFemale reproductive tractFunction of ARID1ARadiation therapyTumor-suppressive actionAtypical hyperplasiaARID1A mutationsARID1A deficiencyTherapeutic vulnerabilitiesChemotherapeutic agentsGenetic alterationsImmune modulationClinical evidenceARID1ASignaling pathway interactionsSuppressive actionEndoplasmic reticulumProtein expressionCancerSpatial mapping of hepatic ER and mitochondria architecture reveals zonated remodeling in fasting and obesity
Parlakgül G, Pang S, Artico L, Min N, Cagampan E, Villa R, Goncalves R, Lee G, Xu C, Hotamışlıgil G, Arruda A. Spatial mapping of hepatic ER and mitochondria architecture reveals zonated remodeling in fasting and obesity. Nature Communications 2024, 15: 3982. PMID: 38729945, PMCID: PMC11087507, DOI: 10.1038/s41467-024-48272-7.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumER-mitochondria interactionsSubcellular spatial organizationER-mitochondriaER sheetsNutritional fluctuationsFatty acid oxidationNutrient availabilityHepatic fatty acid oxidationMetabolic flexibilityVolume electron microscopyHepatic ERMitochondriaLiver zonationSpatial organizationAcid oxidationPericentral hepatocytesHepatocytesMolecular architectureRibosomeProtein1ReticulumRemodelingZonationInteractionProtein condensates in the the secretory pathway: Unraveling biophysical interactions and function
Campelo F, Lillo J, von Blume J. Protein condensates in the the secretory pathway: Unraveling biophysical interactions and function. Biophysical Journal 2024, 123: 1531-1541. PMID: 38698644, PMCID: PMC11214006, DOI: 10.1016/j.bpj.2024.04.031.Peer-Reviewed Original ResearchSecretory pathwayProtein condensatesGolgi apparatusCellular processesEndoplasmic reticulumMembraneless organellesBiomolecular condensatesCellular consequencesCellular organizationBiochemical reactionsFunctional significanceProteinMembrane boundariesBiophysical interactionsPathwayMembraneSpecific componentsGolgiOrganellesReticulumOrganizationSecretoryCondensation interactionInteractionPhase separation phenomenonVolume 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 ERLipid scrambling is a general feature of protein insertases
Li D, Rocha-Roa C, Schilling M, Reinisch K, Vanni S. Lipid scrambling is a general feature of protein insertases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2319476121. PMID: 38621120, PMCID: PMC11047089, DOI: 10.1073/pnas.2319476121.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsEndoplasmic reticulumMembrane proteinsPolypeptide chainLipid scramblingNascent polypeptide chainsVesicle traffickingBiochemical reconstitutionCytosolic leafletProtein insertionMembrane expansionInsertaseMembrane dynamicsHydrophilic grooveHydrophobic membrane interiorScramblaseProteinLipidMembraneBilayer leafletsMembrane interiorOrganellesReticulumPolypeptideTraffickingCOPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites
Liao Y, Pang S, Li W, Shtengel G, Choi H, Schaefer K, Xu C, Lippincott-Schwartz J. COPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites. Developmental Cell 2024, 59: 1410-1424.e4. PMID: 38593803, DOI: 10.1016/j.devcel.2024.03.027.Peer-Reviewed Original ResearchEndoplasmic reticulum exit sitesER exit sitesAmino acid starvationPurified recombinant componentsExit siteProtein sortingSecretory pathwayMammalian cellsNutrient stressCellular conditionsEndoplasmic reticulumGiant unilamellar vesiclesTubular outgrowthsESCRTMicroautophagyNutrient stressorsALG2COPIILysosomesPathwayMTOR inhibitionUnilamellar vesiclesRecombinant componentsFocused Ion Beam Scanning Electron MicroscopyIon beam scanning electron microscopyBridge-like lipid transfer protein family member 2 suppresses ciliogenesis
Parolek J, Burd C. Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis. Molecular Biology Of The Cell 2024, 35: br11. PMID: 38536441, PMCID: PMC11151097, DOI: 10.1091/mbc.e24-02-0065.Peer-Reviewed Original ResearchConceptsLipid transfer proteinsFamily member 2RPE-1 cellsSuppressed ciliogenesisTubular endosomal networkMembrane contact sitesNegative regulator of ciliogenesisRegulator of ciliogenesisDrosophila melanogaster</i>Evolutionary conserved proteinMember 2Primary cilium biogenesisRPE-1Endosomal networkGenetic interactionsTubular endosomesCilium biogenesisProtein familyStructure predictionContact sitesEndoplasmic reticulumDomain-containingPreweaning lethalityNegative regulatorCiliogenesis
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