2024
Ezrin drives adaptation of monocytes to the inflamed lung microenvironment
Gudneppanavar R, Di Pietro C, H Öz H, Zhang P, Cheng E, Huang P, Tebaldi T, Biancon G, Halene S, Hoppe A, Kim C, Gonzalez A, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. Cell Death & Disease 2024, 15: 864. PMID: 39613751, PMCID: PMC11607083, DOI: 10.1038/s41419-024-07255-8.Peer-Reviewed Original ResearchConceptsActivation of focal adhesion kinaseExtracellular matrixActin-binding proteinsFocal adhesion kinaseLung extracellular matrixKnock-out mouse modelProtein kinase signalingCortical cytoskeletonLoss of ezrinKinase signalingPlasma membraneCell migrationSignaling pathwayEzrinResponse to lipopolysaccharideTissue-resident macrophagesMouse modelLipopolysaccharideCytoskeletonEzrin expressionLung microenvironmentKinaseMonocyte recruitmentProteinAktCofilin-Mediated Filament Softening and Crosslinking Counterbalance to Enhance Actin Network Flexibility
Sun Z, Murrell M. Cofilin-Mediated Filament Softening and Crosslinking Counterbalance to Enhance Actin Network Flexibility. Physical Review Letters 2024, 133: 218402. PMID: 39642486, DOI: 10.1103/physrevlett.133.218402.Peer-Reviewed Original ResearchActin-binding proteinsF-actin networkF-actinCrosslinking proteinsF-actin crosslinking proteinCrosslinks F-actinF-actin filamentsTransmission of mechanical forcesCofilin concentrationFilamentous-actinAccessory proteinsCell cytoskeletonCell divisionCell shapeCofilinBinding proteinCell migrationFilament flexibilityProteinDisulfide bondsFilament levelFilamentsCellsMechanical forcesLow pHA Short Isoform of Tensin1 Is a Novel Regulator of F-Actin Assembly in Human Erythroblasts That Promotes Enucleation
Fowler V, Ghosh A, Coffin M, Diaz D, Schulz V, Gallagher P. A Short Isoform of Tensin1 Is a Novel Regulator of F-Actin Assembly in Human Erythroblasts That Promotes Enucleation. Blood 2024, 144: 535-535. DOI: 10.1182/blood-2024-210773.Peer-Reviewed Original ResearchRegulation of F-actin assemblyF-actin assemblyF-actinATAC-peaksH3K27 acetylationN-terminal actin-binding domainErythroid differentiationEnucleated cellsActin-binding domainActin-nucleating factorsF-actin cablesActin-binding proteinsTerminal differentiationActin filament polymerizationC-terminal SH2Translation start siteAssemble F-actinFocal adhesion formationDetect F-actinIncreased chromatin accessibilityErythroid terminal differentiationMolecular regulatory mechanismsSpectrin membrane skeletonMRNA translational start siteReduced F-actin
2019
Phactr1 regulates Slack (KCNT1) channels via protein phosphatase 1 (PP1)
Ali SR, Malone TJ, Zhang Y, Prechova M, Kaczmarek LK. Phactr1 regulates Slack (KCNT1) channels via protein phosphatase 1 (PP1). The FASEB Journal 2019, 34: 1591-1601. PMID: 31914597, PMCID: PMC6956700, DOI: 10.1096/fj.201902366r.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Phosphatase 1Binding of PP1C-terminusCytoplasmic signaling proteinsCytoplasmic C-terminusActin-binding proteinsSlack channelsPKC phosphorylation sitesPhosphoprotein substratesDisease-causing mutationsPhosphorylation sitesSignaling proteinsSlack currentsHuman mutationsSodium-activated potassium channelsPHACTR1Slack genePotassium channelsProteinActinMutationsPatch-clamp recordingsCentral nervous systemMutants
2014
Spire and Formin 2 Synergize and Antagonize in Regulating Actin Assembly in Meiosis by a Ping-Pong Mechanism
Montaville P, Jégou A, Pernier J, Compper C, Guichard B, Mogessie B, Schuh M, Romet-Lemonne G, Carlier M. Spire and Formin 2 Synergize and Antagonize in Regulating Actin Assembly in Meiosis by a Ping-Pong Mechanism. PLOS Biology 2014, 12: e1001795. PMID: 24586110, PMCID: PMC3934834, DOI: 10.1371/journal.pbio.1001795.Peer-Reviewed Original ResearchConceptsBarbed endsCaps filament barbed endsFilament barbed endsRegulate actin assemblyActin assembly dynamicsActin-binding proteinsRab11a-positive vesiclesPresence of actinPing-pong mechanismMechanisms of regulationActin assemblyActin meshworkFormin 2Fmn2ForminBinding proteinAssembly dynamicsArrested growthMolecular mechanismsActinMeiotic spindleProfilinMammalian oocytesProcess assemblyMouse oocytes
2012
Filamins in Mechanosensing and Signaling
Razinia Z, Mäkelä T, Ylänne J, Calderwood DA. Filamins in Mechanosensing and Signaling. Annual Review Of Biophysics 2012, 41: 227-246. PMID: 22404683, PMCID: PMC5508560, DOI: 10.1146/annurev-biophys-050511-102252.Peer-Reviewed Original ResearchConceptsPlasma membraneActin filamentsActin-binding proteinsExtracellular matrix connectionsCortical rigidityActin cytoskeletonCellular functionsCell cortexTranscription factorsTransmembrane receptorsAdhesion proteinsCell shapeFilaminIon channelsDiverse arrayFunctional evidenceEssential roleProteinMatrix connectionsPhysical forcesMembraneFilamentsCytoskeletalMechanosensingCytoskeletonFilamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells
Baldassarre M, Razinia Z, Brahme NN, Buccione R, Calderwood DA. Filamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells. Journal Of Cell Science 2012, 125: 3858-3869. PMID: 22595522, PMCID: PMC3462082, DOI: 10.1242/jcs.104018.Peer-Reviewed Original ResearchMeSH KeywordsActinsCell AdhesionCell Line, TumorCell MovementContractile ProteinsEnzyme ActivationExtracellular MatrixFibrosarcomaFilaminsGene Knockdown TechniquesHumansIntegrinsMatrix Metalloproteinase 14Matrix Metalloproteinase 2Microfilament ProteinsNeoplasm InvasivenessPhenotypeProtein Structure, TertiaryConceptsFilamin AActin cytoskeletonCell invasionActin-binding domainCell surface adhesion proteinsControls cell motilityActin-binding proteinsIntegrin adhesion receptorsRandom cell migrationAbility of cellsArray of intracellularBreast cancer lossSurface adhesion proteinsHuman fibrosarcoma cellsExtracellular matrix degradationMatrix metalloproteinase activityFilamin expressionKnockdown cellsAdhesion proteinsCell motilityMetalloproteinase activityActin filamentsAdhesion receptorsFilaminECM remodeling
2009
Filamins Regulate Cell Spreading and Initiation of Cell Migration
Baldassarre M, Razinia Z, Burande CF, Lamsoul I, Lutz PG, Calderwood DA. Filamins Regulate Cell Spreading and Initiation of Cell Migration. PLOS ONE 2009, 4: e7830. PMID: 19915675, PMCID: PMC2773003, DOI: 10.1371/journal.pone.0007830.Peer-Reviewed Original ResearchConceptsCell spreadingLarge actin-binding proteinCell biological analysesCell migrationActin-binding proteinsLoss of FlnAShRNA-mediated knockdownInitiation of migrationInhibition of initiationRecent knockout studiesProteasomal degradationKnockdown cellsInitiation of motilityKnockout studiesFilaminSingle knockoutImpairs migrationFLNAFLNBBiological analysisKnockdownProteinObserved defectsCellsPeriventricular heterotopiaThe membrane cytoskeletal protein adducin is phosphorylated by protein kinase C in D1 neurons of the nucleus accumbens and dorsal striatum following cocaine administration
Lavaur J, Mineur YS, Picciotto MR. The membrane cytoskeletal protein adducin is phosphorylated by protein kinase C in D1 neurons of the nucleus accumbens and dorsal striatum following cocaine administration. Journal Of Neurochemistry 2009, 111: 1129-1137. PMID: 19780900, PMCID: PMC2810345, DOI: 10.1111/j.1471-4159.2009.06405.x.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsBenzazepinesBenzophenanthridinesCalmodulin-Binding ProteinsCocaineCorpus StriatumDopamine AntagonistsDopamine Uptake InhibitorsDose-Response Relationship, DrugEnzyme InhibitorsGene Expression RegulationGreen Fluorescent ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutNeuronsNucleus AccumbensPhosphorylationProtein Kinase CRacloprideReceptors, Dopamine D1Time FactorsConceptsProtein kinase CAdducin phosphorylationKinase CActin-binding proteinsFamily of proteinsPhosphorylation of adducinCytoskeletal protein adducinActin dynamicsCytoskeletal rearrangementsPhosphorylation stateCytoskeletal proteinsAdducinF-actinPhosphorylationNeuronal cytoskeletonCellular architectureProteinSynaptic functionMorphological changesCytoskeletonMedium spiny neuronsSpectrinRegimen of cocaineActinRegulation
2008
The 3D Structure of Villin as an Unusual F-Actin Crosslinker
Hampton CM, Liu J, Taylor DW, DeRosier DJ, Taylor KA. The 3D Structure of Villin as an Unusual F-Actin Crosslinker. Structure 2008, 16: 1882-1891. PMID: 19081064, PMCID: PMC2782859, DOI: 10.1016/j.str.2008.09.015.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBinding SitesChickensCross-Linking ReagentsImage Processing, Computer-AssistedImaging, Three-DimensionalIntestinesMicrofilament ProteinsModels, MolecularMolecular Sequence DataMolecular WeightMuscle, SkeletalProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRabbitsSequence Homology, Amino AcidConceptsF-actinActin-binding proteinsActin filamentsHomology modelVillinElectron tomographyGelsolinProteinPolar array
2004
Talin controls integrin activation
Calderwood DA. Talin controls integrin activation. Biochemical Society Transactions 2004, 32: 434-437. PMID: 15157154, DOI: 10.1042/bst0320434.Peer-Reviewed Original ResearchConceptsIntegrin beta tailsIntegrin activationCytoplasmic domainBeta tailsMajor actin-binding proteinIntegrin beta cytoplasmic domainsBeta cytoplasmic domainsIntegrin cytoplasmic domainIntegrin activation pathwaysCytoskeletal protein talinIntegrin extracellular domainActin-binding proteinsIntegrin adhesion receptorsBinding of talinTalin FERM domainIntegrin-binding siteMulticellular organismsPTB domainFERM domainProtein talinExtracellular ligandsTalin expressionRNA interferenceTalinIntracellular signals
2002
UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS
Hudson AM, Cooley L. UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS. Annual Review Of Genetics 2002, 36: 455-488. PMID: 12429700, DOI: 10.1146/annurev.genet.36.052802.114101.Peer-Reviewed Original ResearchConceptsActin-binding proteinsActin cytoskeletonGenetic analysisNew actin-binding proteinCell biological approachesGenetic model systemActin binding proteinsRecent genetic analysesDrosophila ovaryDrosophila oogenesisGenetic screenBiological approachesGenetic resultsProteinCytoskeletonOogenesisModel systemUltrastructural characteristicsActinScreenUnderstandingOvaries
2001
Salmonella entry into host cells: the work in concert of type III secreted effector proteins
Zhou D, Galán J. Salmonella entry into host cells: the work in concert of type III secreted effector proteins. Microbes And Infection 2001, 3: 1293-1298. PMID: 11755417, DOI: 10.1016/s1286-4579(01)01489-7.Peer-Reviewed Original ResearchConceptsActin cytoskeleton rearrangementCytoskeleton rearrangementActin dynamicsHost cellsHost actin dynamicsHost signal transductionType III secretion systemActin-binding proteinsSPI-1 type III secretion systemEffector proteinsSecretion systemSignal transductionActin rearrangementBacterial proteinsSalmonella entryIntestinal epithelial cellsBacterial uptakeCdc42Coordinated stepsProteinEpithelial cellsRacRearrangementCellsTransductionActin-Binding Proteins: An Overview
De La Cruz E. Actin-Binding Proteins: An Overview. Results And Problems In Cell Differentiation 2001, 32: 123-134. PMID: 11131827, DOI: 10.1007/978-3-540-46560-7_9.Peer-Reviewed Original Research
2000
Integrin cytoplasmic domain-binding proteins
Liu S, Calderwood D, Ginsberg M. Integrin cytoplasmic domain-binding proteins. Journal Of Cell Science 2000, 113: 3563-3571. PMID: 11017872, DOI: 10.1242/jcs.113.20.3563.Peer-Reviewed Original ResearchConceptsDomain-binding proteinCytoplasmic domainCellular proteinsIntegrin cytoplasmic domainActin-binding proteinsMore cellular proteinsCell surface receptorsGene regulationCellular functionsTransduce signalsSignal transductionBiological functionsGene expressionFunctional analysisCell adhesionLarge familySurface receptorsProteinCytoskeletonIntegrin chainsIntegrinsBiological responsesPivotal roleMechanical linkImportant roleBiophysical characterization of SipA, an actin‐binding protein from Salmonella enterica
Mitra K, Zhou D, Galán J. Biophysical characterization of SipA, an actin‐binding protein from Salmonella enterica. FEBS Letters 2000, 482: 81-84. PMID: 11018527, DOI: 10.1016/s0014-5793(00)02040-8.Peer-Reviewed Original ResearchConceptsActin dynamicsCoiled-coil domainF-actin stabilityActin-binding proteinsActin cytoskeleton reorganizationNon-phagocytic cellsBacterial entryCytoskeleton reorganizationAdjacent actin monomersC-terminal fragmentBiophysical characterizationF-actinCellular responsesHost cellsBacterial uptakeActin monomersProteinSalmonella entericaHelical conformationSalmonella enterica infectionsIntestinal epitheliumEnterica infectionsEssential stepSIPACells
1999
Drosophila Filamin encoded by the cheerio locus is a component of ovarian ring canals
Sokol N, Cooley L. Drosophila Filamin encoded by the cheerio locus is a component of ovarian ring canals. Current Biology 1999, 9: 1221-1230. PMID: 10556087, DOI: 10.1016/s0960-9822(99)80502-8.Peer-Reviewed Original ResearchConceptsRing canalsDrosophila filaminPlasma membraneFilamentous actinActin filamentsOvarian ring canalsFruit fly DrosophilaLoss of filaminActin-binding domainActin-binding proteinsParallel actin bundlesLocalization of filaminFlow of cytoplasmFly DrosophilaActin structuresFilamin isoformsTransmembrane proteinCell cortexActin arraysContractile ringKelch geneCytoskeletal proteinsCleavage furrowStress fibersActin bundlesRegulation of Neurabin I Interaction with Protein Phosphatase 1 by Phosphorylation †
McAvoy T, Allen P, Obaishi H, Nakanishi H, Takai Y, Greengard P, Nairn A, Hemmings H. Regulation of Neurabin I Interaction with Protein Phosphatase 1 by Phosphorylation †. Biochemistry 1999, 38: 12943-12949. PMID: 10504266, DOI: 10.1021/bi991227d.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Neurabin IPP1 activityPhosphatase 1Two-hybrid interaction analysisActin-binding proteinsCo-immunoprecipitation experimentsMimic phosphorylationSerine 461Phosphorylated residuesGlutathione S-transferaseOverlay assaysFusion proteinSignaling mechanismGamma isoformsCAMP pathwayPhosphorylationS-transferaseProteinTryptic digestPKARegulationHPLC-MS analysisInteraction analysisS461An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contact
1997
Actin-binding membrane proteins identified by F-actin blot overlays.
Luna E, Pestonjamasp K, Cheney R, Strassel C, Lu T, Chia C, Hitt A, Fechheimer M, Furthmayr H, Mooseker M. Actin-binding membrane proteins identified by F-actin blot overlays. Society Of General Physiologists Series 1997, 52: 3-18. PMID: 9210216.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAmino Acid SequenceAnimalsBlotting, WesternBrainBreast NeoplasmsCattleChick EmbryoDictyosteliumElectrophoresis, Polyacrylamide GelHeLa CellsHumansIodine RadioisotopesMammalsMembrane ProteinsMiceMicrofilament ProteinsNeuroblastomaNeuropeptidesNeutrophilsSodium Dodecyl SulfateTumor Cells, CulturedConceptsBlot overlayApparent molecular massMembrane proteinsF-actinF-actin binding proteinMolecular massControl cell shapePeripheral membrane proteinsSpecialized membrane domainsCell-cell adhesionPlasma membrane-enriched fractionActin-binding proteinsMammalian cell linesCell surface extensionsMembrane-enriched fractionMembrane rufflesProtein 4.1Membrane domainsMammalian cellsDictyostelium discoideumSoil amoebaPseudopod dynamicsCell shapeEfficient chemotaxisMembrane bilayer
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