2025
Vimentin filament transport and organization revealed by single-particle tracking and 3D FIB-SEM
Renganathan B, Moore A, Yeo W, Petruncio A, Ackerman D, Weigel A, Team T, Pasolli H, Xu C, Shtengel G, Hess H, Serpinskaya A, Zhang H, Lippincott-Schwartz J, Gelfand V. Vimentin filament transport and organization revealed by single-particle tracking and 3D FIB-SEM. Journal Of Cell Biology 2025, 224: e202406054. PMID: 40062969, PMCID: PMC11893169, DOI: 10.1083/jcb.202406054.Peer-Reviewed Original Research
2024
The T4bSS of Legionella features a two-step secretion pathway with an inner membrane intermediate for secretion of transmembrane effectors
Malmsheimer S, Grin I, Bohn E, Franz-Wachtel M, Macek B, Sahr T, Smollich F, Chetrit D, Meir A, Roy C, Buchrieser C, Wagner S. The T4bSS of Legionella features a two-step secretion pathway with an inner membrane intermediate for secretion of transmembrane effectors. PLOS Pathogens 2024, 20: e1012118. PMID: 39546547, PMCID: PMC11602083, DOI: 10.1371/journal.ppat.1012118.Peer-Reviewed Original ResearchConceptsEukaryotic host cellsEffector proteinsMembrane intermediatesC-terminal secretion signalHost cellsSoluble effector proteinsCytoplasmic sideBacterial inner membraneMechanism of secretionSecretion systemSecretion signalPeriplasmic loopTransmembrane effectorSecretion pathwayT4BSSInner membraneSubcellular locationIntracellular survivalMembrane targetingProtein complexesEfficient translocationBacterial cellsProteomic analysisL. pneumophilaSecretion processLipoarabinomannan mediates localized cell wall integrity during division in mycobacteria
Sparks I, Kado T, Prithviraj M, Nijjer J, Yan J, Morita Y. Lipoarabinomannan mediates localized cell wall integrity during division in mycobacteria. Nature Communications 2024, 15: 2191. PMID: 38467648, PMCID: PMC10928101, DOI: 10.1038/s41467-024-46565-5.Peer-Reviewed Original ResearchConceptsCell wall integrityWall integrityRod cell shapeCell envelope integrityHost-pathogen interactionsCell envelope componentsClinically relevant pathogensAssociated with divisionBiosynthetic mutantsEnvelope integritySubcellular locationMycobacterium smegmatisOld poleMulti-septateCell shapeMutantsBacterial modelRelevant pathogensSeptal placementPhysiological functionsMycobacterium tuberculosisEnvelope componentsMycobacteriaLipoarabinomannanDiderm
2022
Cytoskeletal form and function in mammalian oocytes and zygotes
Dunkley S, Scheffler K, Mogessie B. Cytoskeletal form and function in mammalian oocytes and zygotes. Current Opinion In Cell Biology 2022, 75: 102073. PMID: 35364486, DOI: 10.1016/j.ceb.2022.02.007.Peer-Reviewed Original ResearchConceptsCytoskeletal formActin-microtubule interactionsReproductive cell biologyMammalian oocytesActin polymersMicrotubule cytoskeletonChromosome segregationChromosome structureF-actinSubcellular locationCytoskeletal systemSpindle self-organizationMammalian embryo developmentMicroscopy assaysCell biologyEmbryo developmentZygotesOocytesChromosomeAge-related changesCytoskeletalActinBiology
2020
Signaling Diversity Enabled by Rap1 and cAMP/PKA‐Regulated Plasma Membrane ERK with Distinct Temporal Dynamics
Keyes J, Ganesan A, Molinar-Inglis O, Hamidzadeh A, Ling M, Trejo J, Levchenko A, Zhang J. Signaling Diversity Enabled by Rap1 and cAMP/PKA‐Regulated Plasma Membrane ERK with Distinct Temporal Dynamics. The FASEB Journal 2020, 34: 1-1. DOI: 10.1096/fasebj.2020.34.s1.00680.Peer-Reviewed Original ResearchERK activityTemporal regulationPrecise temporal regulationMembrane protrusion dynamicsSequence-specific motifsSpecific subcellular locationsControl cell morphologyDifferent subcellular compartmentsMultiple cellular processesERK enzymatic activityCAMP/PKAERK biosensorEGF inducesKinase cascadeCellular processesExtracellular signalsSubcellular compartmentsSubcellular locationProtrusion dynamicsSubcellular regionsPlasma membraneSpecific motifsEnzymatic activityCell morphologyRap1
2016
Nop9 is a PUF-like protein that prevents premature cleavage to correctly process pre-18S rRNA
Zhang J, McCann KL, Qiu C, Gonzalez LE, Baserga SJ, Hall TM. Nop9 is a PUF-like protein that prevents premature cleavage to correctly process pre-18S rRNA. Nature Communications 2016, 7: 13085. PMID: 27725644, PMCID: PMC5062617, DOI: 10.1038/ncomms13085.Peer-Reviewed Original ResearchConceptsEukaryotic ribosome biogenesisCorrect subcellular locationRibosome assembly factorsPre-ribosomal RNAPumilio repeatsRibosome biogenesisHuman ribosomopathiesAssembly factorsBiogenesis factorsRepeat proteinsMature rRNASubcellular locationNop9RNA complexCleavage siteRRNATimely cleavageProteinStructural featuresFinal processing stepRibosomopathiesBiogenesisCleavageYeastNuclease
2015
Phosphoinositide 3-Kinase-C2α Regulates Polycystin-2 Ciliary Entry and Protects against Kidney Cyst Formation
Franco I, Margaria JP, De Santis MC, Ranghino A, Monteyne D, Chiaravalli M, Pema M, Campa CC, Ratto E, Gulluni F, Perez-Morga D, Somlo S, Merlo GR, Boletta A, Hirsch E. Phosphoinositide 3-Kinase-C2α Regulates Polycystin-2 Ciliary Entry and Protects against Kidney Cyst Formation. Journal Of The American Society Of Nephrology 2015, 27: 1135-1144. PMID: 26271513, PMCID: PMC4814170, DOI: 10.1681/asn.2014100967.Peer-Reviewed Original ResearchConceptsPI3K-C2αCiliary componentsPolycystin-2Primary ciliaRecycling endosome compartmentKidney cyst formationDuct 3 cellsCiliary entryCilium baseElongation defectsCargo proteinsCilium morphogenesisSubcellular locationPhosphoinositide 3Endosome compartmentTubule developmentProliferation signalsCiliary transportCyst formationCystic kidney diseaseIschemia/reperfusion-induced renal damageGenetic modelsCiliaCyst developmentKey mediator
2014
A Promiscuous Lipid-Binding Protein Diversifies the Subcellular Sites of Toll-like Receptor Signal Transduction
Bonham KS, Orzalli MH, Hayashi K, Wolf AI, Glanemann C, Weninger W, Iwasaki A, Knipe DM, Kagan JC. A Promiscuous Lipid-Binding Protein Diversifies the Subcellular Sites of Toll-like Receptor Signal Transduction. Cell 2014, 156: 705-716. PMID: 24529375, PMCID: PMC3951743, DOI: 10.1016/j.cell.2014.01.019.Peer-Reviewed Original ResearchConceptsToll-like receptorsToll-like receptor signal transductionSignal transductionDifferent organellesProinflammatory cytokine expressionSubcellular sitesInnate immune signal transductionInnate immune systemPhosphoinositide-binding domainsImmune signal transductionLipid binding proteinMultiple subcellular locationsReceptor signal transductionCytokine expressionLipid targetsImmune systemInnate immunityHost defenseProtein complexesSubcellular locationPlasma membraneAdaptor TIRAPTIRAPNatural activatorFamily members
2011
The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA
Sim S, Yao J, Weinberg DE, Niessen S, Yates JR, Wolin SL. The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA. RNA 2011, 18: 100-110. PMID: 22114317, PMCID: PMC3261732, DOI: 10.1261/rna.029207.111.Peer-Reviewed Original ResearchConceptsY3 RNASubcellular locationCRM1 inhibitor leptomycin B.RNA-binding proteinExport signalVertebrate nucleiVertebrate cellsY RNAsRNA bindingLeptomycin B.Nuclear exportSubcellular localizationNoncoding RNAsRNA complexZBP1Ro proteinCellular componentsRNACytoplasmProteinNucleusCRM1Complex increasesExportUV irradiation
2010
Ultrastructure and Regulation of Lateralized Connexin43 in the Failing Heart
Hesketh GG, Shah MH, Halperin VL, Cooke CA, Akar FG, Yen TE, Kass DA, Machamer CE, Van Eyk JE, Tomaselli GF. Ultrastructure and Regulation of Lateralized Connexin43 in the Failing Heart. Circulation Research 2010, 106: 1153-1163. PMID: 20167932, PMCID: PMC2896878, DOI: 10.1161/circresaha.108.182147.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagyConnexin 43Disease Models, AnimalDogsGap JunctionsHeart FailureHeart VentriclesHeLa CellsHumansMembrane MicrodomainsMicroscopy, ConfocalMicroscopy, Electron, TransmissionMicrotubule-Associated ProteinsMyocardiumPhosphorylationRatsRats, Sprague-DawleyRecombinant Fusion ProteinsTransfectionConceptsGFP-LC3Gap junctionsLateral membranesDistinct phosphorylated formsGap junction turnoverGap junction internalizationForm of LC3Internalized gap junctionsGap junction proteinJunction turnoverSubcellular locationBiochemical regulationCellular pathwaysMultilamellar membrane structuresEndogenous Cx43Phosphorylated formNeonatal rat ventricular myocytesHeLa cellsIntracellular Cx43Membrane structureJunction proteinsCx43ProteinPotential therapeutic implicationsConnexin43
2007
Regulation of Caveolin‐2 Phosphorylation at Serines 23 and 36
Sowa G, Sessa W. Regulation of Caveolin‐2 Phosphorylation at Serines 23 and 36. The FASEB Journal 2007, 21: a1424-a1424. DOI: 10.1096/fasebj.21.6.a1424-b.Peer-Reviewed Original ResearchLipid rafts/caveolaeSerine 36 phosphorylationRafts/caveolaeSerine 23Cav-2Serine phosphorylationCav-1Phospho-specific antibodiesSubcellular fractionation dataSubcellular fractionation techniquesN-terminal serineEndothelial cellsCaveolar compartmentCaveolae assemblyLipid raftsSubcellular locationRegulated processSerine 36Caveolin-2Human endothelial cellsAdenoviral expressionIntracellular compartmentsPhosphorylationCaveolaeResidues 23
2001
Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization.
Long K, Cedervall T, Walch-Solimena C, Noe D, Huddleston M, Annan R, Wolin S. Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization. RNA 2001, 7: 1589-602. PMID: 11720288, PMCID: PMC1370201.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensBinding SitesCell NucleolusCell NucleusFungal ProteinsMolecular Sequence DataPeptide MappingPhosphorylationProtein IsoformsRibonucleoproteinsRibonucleoproteins, Small NuclearRNARNA StabilityRNA, FungalRNA, TransferRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsS. cerevisiae proteinTwo-dimensional gel electrophoresisRole of phosphorylationPolymerase III transcriptsCerevisiae proteinsNascent RNANascent transcriptsS. pombeSchizosaccharomyces pombeLhp1pPhosphorylation sitesYeast SaccharomycesProtein functionMutant versionSubcellular locationFirst proteinHuman proteinsNuclear phosphoproteinExonucleolytic degradationSerine phosphorylationPhosphorylation statusRNA stabilization
1999
TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1.
Jones S, Ledgerwood E, Prins J, Galbraith J, Johnson D, Pober J, Bradley J. TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1. The Journal Of Immunology 1999, 162: 1042-8. PMID: 9916731, DOI: 10.4049/jimmunol.162.2.1042.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDAortaBrefeldin ACattleCell CompartmentationCell Line, TransformedCell MembraneEndothelium, VascularGolgi ApparatusHumansMicroscopy, ConfocalProteinsReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISubcellular FractionsTNF Receptor-Associated Factor 1TransfectionTumor Necrosis Factor-alphaU937 CellsConceptsTrans-Golgi networkPlasma membraneTNF-R1Golgi regionConfocal immunofluorescence microscopyHuman endothelial cell line ECV304Endothelial cell line ECV304Receptor-mediated endocytosisAdaptor proteinSubcellular localizationSubcellular locationCell fractionationBovine aortic endothelial cellsCoimmunoprecipitation studiesEndothelial cellsTRADDCell line U937Golgi apparatusSubcellular interactionsWestern blot analysisCell extractsMonocyte cell line U937Expression plasmidGolgiImmunofluorescence microscopy
1996
Aromatase Immunoreactivity in Axon Terminals of the Vertebrate Brain
Naftolin F, Horvath T, Jakab R, Leranth C, Harada N, Balthazart J. Aromatase Immunoreactivity in Axon Terminals of the Vertebrate Brain. Neuroendocrinology 1996, 63: 149-155. PMID: 9053779, DOI: 10.1159/000126951.Peer-Reviewed Original ResearchConceptsAxon terminalsAromatase immunoreactivityAxonal processesDifferent vertebrate speciesAdult central nervous systemRole of aromataseSmall clear synaptic vesiclesCentral nervous systemClear synaptic vesiclesVertebrate speciesSubcellular locationMost vertebratesSpecific limbicNeuronal perikaryaAromatase activityElectron microscopic examinationEstrogen synthesisHypothalamic structuresSubcellular distributionSynaptic levelVertebrate brainNervous systemBrain aromataseMolecular biologyIntraneuronal production
1994
Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae.
Burns N, Grimwade B, Ross-Macdonald P, Choi E, Finberg K, Roeder G, Snyder M. Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae. Genes & Development 1994, 8: 1087-1105. PMID: 7926789, DOI: 10.1101/gad.8.9.1087.Peer-Reviewed Original ResearchConceptsFusion proteinFusion geneSubcellular locationGene productsCytoplasmic dotsVegetative growthVegetative cellsSpecific subcellular locationsSpindle pole bodyEncoded gene productsLarge-scale screenOpen reading frameGal fusion proteinLife cycleYeast genesYeast genomeGenomic libraryPole bodyHomozygous diploidsHaploid cellsProtein localizationIndirect immunofluorescence analysisGene disruptionReading frameDNA sequences
1993
Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins.
O'Brien C, Margelot K, Wolin S. Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7250-7254. PMID: 7688474, PMCID: PMC47114, DOI: 10.1073/pnas.90.15.7250.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinSmall ribonucleoproteinHuman Y RNAsSmall RNA moleculesXenopus egg extractsAmino acid sequenceY-RNAsHY3 RNAsVertebrate speciesMammalian cellsRo RNPsSubcellular locationRNA componentCytoplasmic ribonucleoproteinHY5 RNAAdditional proteinsRNA moleculesAcid sequenceHuman RNAEgg extractsEntire proteinConserved stemOocyte cytoplasmRibonucleoproteinAnalysis of the structure and subcellular location of filamentous phage pIV
Russel M, Kaźmierczak B. Analysis of the structure and subcellular location of filamentous phage pIV. Journal Of Bacteriology 1993, 175: 3998-4007. PMID: 8320216, PMCID: PMC204828, DOI: 10.1128/jb.175.13.3998-4007.1993.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseBacterial ProteinsCell CompartmentationColiphagesDNA Mutational AnalysisGene Expression Regulation, BacterialGenes, ViralHeat-Shock ProteinsMembrane ProteinsMutationOperonRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidSpheroplastsSubcellular FractionsViral ProteinsVirus ReplicationConceptsMembrane localization domainIntegral membrane proteinsSubstrate-binding domainAmino-terminal halfCarboxy-terminal halfSeries of genesCell fractionation studiesCytoplasmic domainPhage assemblyDeletion mutantsMembrane proteinsSubcellular locationLocalization domainFusion proteinFractionation studiesFilamentous phagePhosphatase activityFilamentous bacteriophageAlkaline phosphatase activityMissense mutationsProteinAssemblyDomainMutantsGenes
1982
Small RNPs in eucaryotic cells
Hendrick J, Mount S, Rinke J, Wolin S, Rosa M, Gottlieb E, Lerner M, Steitz J. Small RNPs in eucaryotic cells. 1982, 321-328. DOI: 10.1007/978-1-349-06343-7_44.Peer-Reviewed Original ResearchSmall nuclear RNAAbundant small nuclear RNAsRNA-protein complexesEukaryotic cellsSmall RNAsSmall ribonucleoproteinSubcellular locationNuclear RNARNA componentU1 snRNPsEucaryotic cellsComponent RNARibonucleoproteinRNP particlesRNAInitial discoveryProteinPartial characterizationState of maturationSnRNPsCellsSystemic lupus erythematosusDiversityMaturationMetabolism
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