2025
Fast Actin Disassembly and Fimbrin Mechanosensitivity Support Rapid Turnover in a Model of Clathrin‐Mediated Endocytosis
Mousavi S, Lacy M, Li X, Berro J. Fast Actin Disassembly and Fimbrin Mechanosensitivity Support Rapid Turnover in a Model of Clathrin‐Mediated Endocytosis. Cytoskeleton 2025 PMID: 40035221, DOI: 10.1002/cm.22002.Peer-Reviewed Original ResearchClathrin-mediated endocytosisActin filament disassemblyDynamics of actinActin-interacting proteinHigh membrane tensionActin meshworkEndocytic proteinsFilament disassemblyActin disassemblyNascent filamentsActin cytoskeletonEndocytic structuresEukaryotic cellsBinding partnersCellular processesTurgor pressureFimbrinActinRapid turnoverMembrane tensionEndocytosisProteinFilamentsDisassemblyYeast
2024
A role for the kinetochore protein, NUF2, in ribosome biogenesis
brown T, Pichurin J, Parrado C, Kabeche L, Baserga S. A role for the kinetochore protein, NUF2, in ribosome biogenesis. Molecular Biology Of The Cell 2024, 36: ar16. PMID: 39705402, PMCID: PMC11809303, DOI: 10.1091/mbc.e24-08-0337.Peer-Reviewed Original ResearchConceptsPre-rRNA transcriptionNucleolar stress pathwayRibosome biogenesisPre-rRNASiRNA depletionSubunit of RNA polymerase IGenome-wide siRNA screenMCF10A human breast epithelial cellsRNA polymerase IHuman breast epithelial cellsBreast epithelial cellsKinetochore proteinsMitotic kinetochoresEukaryotic cellsPolymerase ISiRNA screenProtein partnersNUF2Sub-complexCell-based assaysProtein componentsRibosomeStress pathwaysTranscriptionProteinBacterial Organelles in Iron Physiology
Ferrara K, Gupta K, Pi H. Bacterial Organelles in Iron Physiology. Molecular Microbiology 2024, 122: 914-928. PMID: 39545931, PMCID: PMC11659020, DOI: 10.1111/mmi.15330.Peer-Reviewed Original ResearchMembrane-bound organellesBacterial organellesFerritin-like proteinsEukaryotic organellesProtein-lipid monolayersEukaryotic cellsProteinaceous shellSpecies-specificBacterial cellsOrganellesProtecting cellsLife formsBiochemical reactionsPhysiological functionsDiverse arrayIron physiologyEnvironmental conditionsLipid bilayerBacteriaEssential micronutrientCellsSpecial structureBiogenesisGeneticsProteinMotion 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
2023
Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases
Robles J, Lou H, Shi G, Pan P, Turk B. Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2316599120. PMID: 37988460, PMCID: PMC10691213, DOI: 10.1073/pnas.2316599120.Peer-Reviewed Original ResearchConceptsExtracellular signal-regulated kinase 2Docking motifERK2 mitogen-activated protein kinaseSignal-regulated kinase 2Protein kinase cascadeMitogen-activated protein kinaseFull-length proteinMAPK substratesEukaryotic cellsKinase cascadeMAPK networkLinear motifsProtein kinaseMotif specificityProteomic librariesDocking siteAcidic residuesKinase 2Diverse stimuliCellular responsesP38αDocking interfaceHigh net chargeMotifSelective interactionA defect in mitochondrial fatty acid synthesis impairs iron metabolism and causes elevated ceramide levels
Dutta D, Kanca O, Byeon S, Marcogliese P, Zuo Z, Shridharan R, Park J, Lin G, Ge M, Heimer G, Kohler J, Wheeler M, Kaipparettu B, Pandey A, Bellen H. A defect in mitochondrial fatty acid synthesis impairs iron metabolism and causes elevated ceramide levels. Nature Metabolism 2023, 5: 1595-1614. PMID: 37653044, PMCID: PMC11151872, DOI: 10.1038/s42255-023-00873-0.Peer-Reviewed Original ResearchConceptsFatty acid synthesisFe-S cluster biogenesisMitochondrial fatty acid synthesisCeramide levelsMost eukaryotic cellsElevated ceramide levelsIron metabolismCluster biogenesisEukaryotic cellsLoss of functionCellular lipidomeEnoyl coenzymeNeurodegenerative phenotypeIron homeostasisHuman-derived fibroblastsMechanistic linkAcid synthesisCeramideMECRMetabolismNeurodegenerationMtFASBiogenesisLast stepMitochondriaA dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin
Sahu S, Ekundayo B, Kumar A, Bleichert F. A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. The EMBO Journal 2023, 42: embj2023114654. PMID: 37551430, PMCID: PMC10505921, DOI: 10.15252/embj.2023114654.Peer-Reviewed Original ResearchConceptsOrigin recognition complexH4K20 trimethylationHeterochromatin replicationRecognition complexCryo-electron microscopy structureLocal chromatin environmentSpecific histone marksSpecific chromatin contextsMcm2-7 loadingTernary complex assemblyChromatin environmentChromatin marksChromatin contextHistone marksHistone modificationsReplication initiationEukaryotic cellsMicroscopy structureChromatin condensatesORC recruitmentDNA replicationMammalian cellsNucleosomal DNAAromatic cageComplex assemblyRBG Motif Bridge-Like Lipid Transport Proteins: Structure, Functions, and Open Questions
Hanna M, Guillén-Samander A, De Camilli P. RBG Motif Bridge-Like Lipid Transport Proteins: Structure, Functions, and Open Questions. Annual Review Of Cell And Developmental Biology 2023, 39: 409-434. PMID: 37406299, DOI: 10.1146/annurev-cellbio-120420-014634.Peer-Reviewed Original ResearchLipid transfer proteinMembrane contact sitesVesicle-mediated trafficTransport of lipidsPutative physiological roleEukaryotic cellsEndocytic pathwayContact sitesLipid transportPhysiological roleTransfer proteinProteinHydrophobic channelRod-like structureLipidsEntire lengthDevelopmental disordersCytosolMutationsNew familyTransportPathwayMechanismMembraneCellsMolecular Biology of Cytoplasmic Incompatibility Caused by Wolbachia Endosymbionts
Hochstrasser M. Molecular Biology of Cytoplasmic Incompatibility Caused by Wolbachia Endosymbionts. Annual Review Of Microbiology 2023, 77: 299-316. PMID: 37285552, DOI: 10.1146/annurev-micro-041020-024616.Peer-Reviewed Original ResearchConceptsCytoplasmic incompatibilityMale killingHost ubiquitin systemEndosymbiotic bacteriaFemale germlineEukaryotic cellsCognate partnersEmbryonic lethalityBicistronic operonUbiquitin systemDownstream genesWolbachia endosymbiontReproductive advantageCI inductionMolecular biologyInfected femalesEndosymbiontsInfections of malesReproductive alterationsDeubiquitylaseDeubiquitylasesOperonParthenogenesisArthropodsGermlineInsights of Endocytosis Signaling in Health and Disease
Pathak C, Vaidya F, Waghela B, Jaiswara P, Gupta V, Kumar A, Rajendran B, Ranjan K. Insights of Endocytosis Signaling in Health and Disease. International Journal Of Molecular Sciences 2023, 24: 2971. PMID: 36769293, PMCID: PMC9918140, DOI: 10.3390/ijms24032971.Peer-Reviewed Original ResearchConceptsEndocytic machineryPlasma membraneCellular defenseFundamental cellular machinerySignal transduction modulesDifferent cellular compartmentsVital physiological processesProcess of endocytosisEndocytic proteinsIndependent endocytosisEndocytosis machineryTransduction modulesEukaryotic cellsCaveolar pathwayCellular machineryMammalian cellsEndocytic pathwayCell divisionCellular compartmentsComplex proteinsFunctional characterizationPhysiological processesMachinery resultsHuman diseasesEndocytosisSyntaxin 11 Contributes to the Interferon-Inducible Restriction of Coxiella burnetii Intracellular Infection
Ganesan S, Alvarez N, Steiner S, Fowler K, Corona A, Roy C. Syntaxin 11 Contributes to the Interferon-Inducible Restriction of Coxiella burnetii Intracellular Infection. MBio 2023, 14: e03545-22. PMID: 36728431, PMCID: PMC9972978, DOI: 10.1128/mbio.03545-22.Peer-Reviewed Original ResearchConceptsC. burnetii replicationSNARE proteinsHost cellsSyntaxin-11Cell-autonomous responsesIntracellular pathogensMembrane fusion eventsLysosome-derived organellesDefense mechanismsModel bacterial pathogenMultiple cell typesEukaryotic cellsDefense pathwaysDelivery of cargoReplication of pathogensHuman proteinsFusion eventsDissemination of pathogensFusion pathwayHost proteinsIntrinsic defense mechanismsHost vesiclesHost restriction factorsStable expressionSubcellular organelles
2022
Comparison of the PF07598-Encoded Virulence-Modifying Proteins of L. interrogans and L. borgpetersenii
Vieira D, Chaurasia R, Vinetz J. Comparison of the PF07598-Encoded Virulence-Modifying Proteins of L. interrogans and L. borgpetersenii. Tropical Medicine And Infectious Disease 2022, 8: 14. PMID: 36668921, PMCID: PMC9863803, DOI: 10.3390/tropicalmed8010014.Peer-Reviewed Original ResearchVM proteinsEukaryotic cellsGene familyEnvironmental nichesDifferent cladesMammalian hostsSeverity of outbreaksVirulence effectsCellular pathogenesisHuman pathogensMediated TransmissionLeptospiral speciesParalogsPathogenic groupsProteinVaccine-mediated preventionSpeciesL. interrogansL. borgpeterseniiProtein exotoxinsNew strainFatal leptospirosisTarget cellsLeptospirosis pathogenesisInfectious diseasesAssembly and architecture of the type III secretion sorting platform
Soto J, Galán J, Lara-Tejero M. Assembly and architecture of the type III secretion sorting platform. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2218010119. PMID: 36512499, PMCID: PMC9907115, DOI: 10.1073/pnas.2218010119.Peer-Reviewed Original ResearchConceptsType III secretion machinesType III secretion systemTarget eukaryotic cellsType III secretionSecretion of proteinsBacterial nanomachinesSecretion machineEukaryotic cellsExport pathwayImportant bacterial pathogensSecretion systemBacterial structureAntivirulence strategiesCoordinated mechanismFunctional complexityBacterial pathogensGenetic deletionStructure modelingProtein deliveryAssemblyRational developmentCross-linking strategyAssembly processProteinDeletion
2021
Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport
Leonzino M, Reinisch KM, De Camilli P. Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport. Biochimica Et Biophysica Acta (BBA) - Molecular And Cell Biology Of Lipids 2021, 1866: 159003. PMID: 34216812, PMCID: PMC8325632, DOI: 10.1016/j.bbalip.2021.159003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagosomesAutophagy-Related ProteinsCryoelectron MicroscopyDisease Models, AnimalEukaryotic CellsHeredodegenerative Disorders, Nervous SystemHumansHydrophobic and Hydrophilic InteractionsLipid BilayersLipid MetabolismMitochondrial MembranesMutationProtein DomainsStructure-Activity RelationshipVesicular Transport ProteinsYeastsConceptsLipid transportMembrane contact sitesDomain protein familyOccurrence of proteinsVPS13 proteinsEukaryotic cellsNumerous proteinsProtein familyIntracellular membranesProtein bridgeHydrophobic grooveContact sitesMembrane growthLipid transferBilayer lipidsNovel mechanismVps13New mechanismProteinLipidsAtg2OrganellesAdjacent bilayersDiscoveryMechanismIncreased numbers of nucleoli in a genome-wide RNAi screen reveal proteins that link the cell cycle to RNA polymerase I transcription
Ogawa LM, Buhagiar AF, Abriola L, Leland BA, Surovtseva YV, Baserga SJ. Increased numbers of nucleoli in a genome-wide RNAi screen reveal proteins that link the cell cycle to RNA polymerase I transcription. Molecular Biology Of The Cell 2021, 32: 956-973. PMID: 33689394, PMCID: PMC8108525, DOI: 10.1091/mbc.e20-10-0670.Peer-Reviewed Original ResearchConceptsRNA polymerase INumber of nucleoliRibosome biogenesisNucleolar organizer regionsPolymerase ICell cycleRNA polymerase I transcriptionPolymerase I transcriptionCell cycle regulationHigh-throughput quantitative imagingHuman diploid genomeIdentification of proteinsEukaryotic cellsG2/M phaseDiploid genomeNuclear condensatesRibosomal DNACycle regulationHuman breast epithelial cell lineBreast epithelial cell lineI transcriptionNovel regulatorEpithelial cell lineCycle progressionFunctional analysisPopulation genomics in the arboviral vector Aedes aegypti reveals the genomic architecture and evolution of endogenous viral elements
Crava C, Varghese F, Pischedda E, Halbach R, Palatini U, Marconcini M, Gasmi L, Redmond S, Afrane Y, Ayala D, Paupy C, Carballar‐Lejarazu R, Miesen P, van Rij R, Bonizzoni M. Population genomics in the arboviral vector Aedes aegypti reveals the genomic architecture and evolution of endogenous viral elements. Molecular Ecology 2021, 30: 1594-1611. PMID: 33432714, PMCID: PMC8048955, DOI: 10.1111/mec.15798.Peer-Reviewed Original ResearchConceptsPIWI-interacting RNAsArboviral vector Aedes aegyptiEndogenous viral elementsPopulation genomicsGenomic architectureViral elementsVector Aedes aegyptiPiRNA-mediated silencingNonretroviral RNA virusesGenome-wide screenHorizontal gene transferSequence-specific mechanismWild-caught mosquitoesA. aegyptiEndogenization eventsAedes aegyptiAdaptive evolutionPiRNA clustersEukaryotic cellsGermline cellsTransposable elementsGeographical populationsHost genomeHost functionsCognate virus
2020
The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform
Muthuramalingam M, Whittier SK, Lovell S, Battaile KP, Tachiyama S, Johnson DK, Picking WL, Picking WD. The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform. Journal Of Molecular Biology 2020, 432: 166693. PMID: 33122003, PMCID: PMC10550303, DOI: 10.1016/j.jmb.2020.10.027.Peer-Reviewed Original ResearchConceptsInner membrane ringBasal bodiesCytoplasmic domainSorting platformFirst high-resolution structureType III secretion systemCytoplasmic sorting platformTwo-hybrid analysisGram-negative bacterial pathogensProtein family membersNormal cellular functionHigh-resolution structuresAtomic resolution modelsHelix-rich structureEukaryotic cellsT3SS apparatusAdaptor proteinCellular functionsSecretion systemMembrane ringMechanistic interfaceTip complexExternal needleRadial spokesProteinPathogenesis and promising therapeutics of Alzheimer disease through eIF2α pathway and correspondent kinases
Moradi Majd R, Mayeli M, Rahmani F. Pathogenesis and promising therapeutics of Alzheimer disease through eIF2α pathway and correspondent kinases. Metabolic Brain Disease 2020, 35: 1241-1250. PMID: 32681467, DOI: 10.1007/s11011-020-00600-8.Peer-Reviewed Original ResearchConceptsHeme-regulated inhibitor kinasePKR-like endoplasmic reticulum kinaseActivating Transcription Factor 4Double-stranded RNA-activated protein kinasePathological hallmarks of ADEukaryotic initiation factor 2RNA-activated protein kinaseInitiation factor 2Hallmarks of ADRegulation of protein synthesisEndoplasmic reticulum kinaseAlzheimer's diseaseBeta-amyloidogenesisSer-51Transcription factor 4Tau phosphorylationEukaryotic cellsTherapeutics of Alzheimer's diseaseB-secretaseProtein kinasePathway inductionPathological hallmarkKinaseProtein synthesisPhosphorylationEstablishing rod shape from spherical, peptidoglycan-deficient bacterial spores
Zhang H, Mulholland GA, Seef S, Zhu S, Liu J, Mignot T, Nan B. Establishing rod shape from spherical, peptidoglycan-deficient bacterial spores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 14444-14452. PMID: 32513721, PMCID: PMC7321990, DOI: 10.1073/pnas.2001384117.Peer-Reviewed Original ResearchConceptsBacterial actin homolog MreBFuture cell polesActin homolog MreBGTPase-activating proteinsMolecular motorsGram-negative bacteriumCell polesEukaryotic cellsSynthesis complexSpherical sporesWalled cellsRod shapeMglBMglAPG growthSporesMreBBacterial sporesGTPaseCellsCytoskeletonMyxococcusPeptidoglycanProteinBacteriumAn in vitro mimic of in‐cell solvation for protein folding studies
Davis CM, Deutsch J, Gruebele M. An in vitro mimic of in‐cell solvation for protein folding studies. Protein Science 2020, 29: 1046-1054. PMID: 31994240, PMCID: PMC7096716, DOI: 10.1002/pro.3833.Peer-Reviewed Original ResearchConceptsPhosphoglycerate kinaseLysis bufferCytoplasmic protein interactionsSignificant nonadditive effectsVariety of proteinsProtein folding studiesEukaryotic cellsProtein foldingProtein interactionsCellular crowdingProtein-like sequencesEffect of FicollFolding studiesHydrophobic patchVariable major protein-like sequenceNonadditive effectsCellular effectsProteinCell environmentInert macromoleculesBiomolecular interactionsCellsTest tubeSmall crowdersMimics
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply