2025
Nanoscopy reveals integrin clustering reliant on kindlin-3 but not talin-1
Wu Y, Cao Z, Liu W, Cahoon J, Wang K, Wang P, Hu L, Chen Y, Moser M, Vella A, Ley K, Wen L, Fan Z. Nanoscopy reveals integrin clustering reliant on kindlin-3 but not talin-1. Cell Communication And Signaling 2025, 23: 12. PMID: 39773732, PMCID: PMC11707915, DOI: 10.1186/s12964-024-02024-8.Peer-Reviewed Original Research
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 pathwaysTranscriptionProteinEzrin 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 recruitmentProteinAktIdentification of coilin interactors reveals coordinated control of Cajal body number and structure
Escayola D, Zhang C, Nischwitz E, Schärfen L, Dörner K, Straube K, Kutay U, Butter F, Neugebauer K. Identification of coilin interactors reveals coordinated control of Cajal body number and structure. Journal Of Cell Biology 2024, 224: e202305081. PMID: 39602297, PMCID: PMC11602656, DOI: 10.1083/jcb.202305081.Peer-Reviewed Original ResearchConceptsCajal bodiesSurvival motor neuron proteinCB assemblyModulating posttranslational modificationsRegulate RNA processingProtein interactorsProximity biotinylationRNA processingGenetic lociPosttranslational modificationsGene activationTranscription factorsFunctional screeningBiomolecular condensatesCoilinNeuronal proteinsCell nucleiProteinNuclear levelsNuclear positivityCB componentsCB numberBody numberAssemblyRibosome
2023
Sequence variants in different genes underlying Bardet-Biedl syndrome in four consanguineous families
Ali A, Abdullah, Bilal M, Mis E, Lakhani S, Ahmad W, Ullah I. Sequence variants in different genes underlying Bardet-Biedl syndrome in four consanguineous families. Molecular Biology Reports 2023, 50: 9963-9970. PMID: 37897612, DOI: 10.1007/s11033-023-08816-4.Peer-Reviewed Original ResearchMeSH KeywordsBardet-Biedl SyndromeConsanguinityCytoskeletal ProteinsDNA Mutational AnalysisHumansMutationPedigreePhosphate-Binding ProteinsConceptsUnique inheritance patternConsanguineous familyPakistani consanguineous familyMKK genesDifferent genesBBS7 geneBardet-Biedl syndromeWhole-exome sequencingRod-cone dystrophyBBS genesGenesCompound heterozygous variantsNovel homozygous variantHeterogeneous congenital disorderInheritance patternRelated phenotypesExome sequencingClinical manifestationsMutational screeningRenal abnormalitiesMutation spectrumCognitive impairmentHeterozygous variantsPakistani populationHomozygous variant
2022
Fibroblasts secrete fibronectin under lamellipodia in a microtubule- and myosin II–dependent fashion
Huet-Calderwood C, Rivera-Molina F, Toomre D, Calderwood D. Fibroblasts secrete fibronectin under lamellipodia in a microtubule- and myosin II–dependent fashion. Journal Of Cell Biology 2022, 222: e202204100. PMID: 36416725, PMCID: PMC9699186, DOI: 10.1083/jcb.202204100.Peer-Reviewed Original ResearchMeSH KeywordsCytoskeletal ProteinsExocytosisExtracellular MatrixFibroblastsFibronectinsIntegrinsMicrotubulesMyosin Type IIPseudopodiaConceptsFN secretionFocal adhesion dynamicsExtracellular matrixFocal adhesion formationSites of exocytosisLive-cell microscopyIntegrin-independent mannerCytoskeletal dynamicsFocal adhesionsAdhesion dynamicsRegulatory componentsMyosin IIIntact microtubulesCell polarizationCell adhesionIntegrin receptorsFN depositionLamellipodiaMicrotubulesFibronectinAdhesion formationNew adhesion formationFibroblastsII-dependent fashionCellsAutoinhibition of the GEF activity of cytoskeletal regulatory protein Trio is disrupted in neurodevelopmental disorder-related genetic variants
Bircher JE, Corcoran EE, Lam TT, Trnka MJ, Koleske AJ. Autoinhibition of the GEF activity of cytoskeletal regulatory protein Trio is disrupted in neurodevelopmental disorder-related genetic variants. Journal Of Biological Chemistry 2022, 298: 102361. PMID: 35963430, PMCID: PMC9467883, DOI: 10.1016/j.jbc.2022.102361.Peer-Reviewed Original ResearchMeSH KeywordsCytoskeletal ProteinsCytoskeletonGuanineHumansMonomeric GTP-Binding ProteinsNeurodevelopmental DisordersSpectrinConceptsSpectrin repeatsGEF1 domainPleckstrin homology regionExchange factor domainKey regulatory mechanismCytoskeletal regulatory proteinsSmall GTPase Rac1Autoinhibitory constraintsAccessory domainsNeurodevelopmental disordersGEF activityMultiple neurodevelopmental disordersKinase domainHomology regionProtein TrioGTPase Rac1Regulatory proteinsRegulatory mechanismsFactor domainSRS-6Genetic variantsGef1Disease variantsEnzymatic activityBio-Layer InterferometryActivation of the CaMKII-Sarm1-ASK1-p38 MAP kinase pathway protects against axon degeneration caused by loss of mitochondria
Ding C, Wu Y, Dabas H, Hammarlund M. Activation of the CaMKII-Sarm1-ASK1-p38 MAP kinase pathway protects against axon degeneration caused by loss of mitochondria. ELife 2022, 11: e73557. PMID: 35285800, PMCID: PMC8920508, DOI: 10.7554/elife.73557.Peer-Reviewed Original ResearchConceptsMAPK pathwayLoss of mitochondriaMitochondrial defectsUnbiased genetic screenMAP kinase pathwayCell-specific activationTrafficking complexGenetic screenCEBP-1Kinase pathwayUnderlying cellular mechanismsCellular mechanismsL-type voltage-gated calcium channelsMitochondriaVoltage-gated calcium channelsPathwayUNCAxon degenerationCaenorhabditisActivationCalcium channelsFurther analysisTraffickingSuppressesCaMKIIWhy are keratins important?
Fisk J, Nebert D. Why are keratins important? Human Genomics 2022, 16: 4. PMID: 35094700, PMCID: PMC8801120, DOI: 10.1186/s40246-022-00379-y.Peer-Reviewed Original Research
2021
MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells
Jeong J, Shin JH, Li W, Hong JY, Lim J, Hwang JY, Chung JJ, Yan Q, Liu Y, Choi J, Wysolmerski J. MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells. Cell Reports 2021, 37: 110160. PMID: 34965434, PMCID: PMC8762588, DOI: 10.1016/j.celrep.2021.110160.Peer-Reviewed Original ResearchMeSH KeywordsAntineoplastic Agents, ImmunologicalBreast NeoplasmsCell ProliferationCytoskeletal ProteinsDrug Resistance, NeoplasmEndocytosisFemaleHumansMembrane MicrodomainsMyelin and Lymphocyte-Associated Proteolipid ProteinsPhosphoproteinsPlasma Membrane Calcium-Transporting ATPasesReceptor, ErbB-2Sodium-Hydrogen ExchangersTrastuzumabTumor Cells, CulturedConceptsLipid raft formationBreast cancer cellsLipid raftsLipid raft resident proteinsCancer cellsRaft formationRaft-resident proteinsProximity ligation assayProtein complexesMembrane protrusionsProtein interactionsPlasma membraneLigation assayMAL2Membrane stabilityStructural organizationPotential therapeutic targetPhysical interactionMembrane retentionProteinRaftsTherapeutic targetCellsIntracellular calcium concentrationLow intracellular calcium concentrationEpistatic interaction of PDE4DIP and DES mutations in familial atrial fibrillation with slow conduction
Ziki M, Bhat N, Neogi A, Driscoll TP, Ugwu N, Liu Y, Smith E, Abboud JM, Chouairi S, Schwartz MA, Akar JG, Mani A. Epistatic interaction of PDE4DIP and DES mutations in familial atrial fibrillation with slow conduction. Human Mutation 2021, 42: 1279-1293. PMID: 34289528, PMCID: PMC8434967, DOI: 10.1002/humu.24265.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAtrial FibrillationCardiomyopathy, DilatedCytoskeletal ProteinsDesminExome SequencingHumansMutationPenetranceConceptsEarly-onset atrial fibrillationAtrial fibrillationHeart blockFamilial atrial fibrillationSlow conductionDES mutationsSlow atrial fibrillationWhole-exome sequencingConduction diseaseIsoproterenol stimulationExome sequencingGenetic causePathogenic mutationsPDE4DIPReduced colocalizationHigh penetranceGenetic screeningUnrelated kindredsFibrillationPKA phosphorylationDesmin geneEpistatic interactionsT substitutionKindredsPDE4DRetinal waves prime visual motion detection by simulating future optic flow
Ge X, Zhang K, Gribizis A, Hamodi AS, Sabino AM, Crair MC. Retinal waves prime visual motion detection by simulating future optic flow. Science 2021, 373 PMID: 34437090, PMCID: PMC8841103, DOI: 10.1126/science.abd0830.Peer-Reviewed Original ResearchConceptsEye-specific segregationSpontaneous retinal wavesVisual response propertiesSpontaneous retinal activityDirection-selective responsesSuperior colliculus neuronsOptic flow patternsRetinal wavesRetinal activityColliculus neuronsRetinal circuitsSpontaneous activityChronic disruptionVisual motion detectionEye openingTransient windowResponse propertiesOptic flowSensory experienceNeuronsStructural insights into the cause of human RSPH4A primary ciliary dyskinesia
Zhao Y, Pinskey J, Lin J, Yin W, Sears P, Daniels L, Zariwala M, Knowles M, Ostrowski L, Nicastro D. Structural insights into the cause of human RSPH4A primary ciliary dyskinesia. Molecular Biology Of The Cell 2021, 32: 1202-1209. PMID: 33852348, PMCID: PMC8351563, DOI: 10.1091/mbc.e20-12-0806.Peer-Reviewed Original ResearchMeSH KeywordsAxonemeCiliaCiliary Motility DisordersCytoskeletal ProteinsElectron Microscope TomographyHumansMutationRespiratory SystemConceptsStructural basisCryo-electron tomographyRadial spokesCentral pair complexUnderlying structural basisAxonemal repeatEukaryotic organellesArch domainThree-dimensional structureSubtomogram averagingOrgan positioningCell motilityStructural insightsPrimary ciliary dyskinesiaCiliaHuman ciliaHuman respiratory ciliaRS1Primary defectStructure determinationCiliary dyskinesiaHuman healthOrganellesFlagellaRepeatsLong noncoding RNA TINCR is a novel regulator of human bronchial epithelial cell differentiation state
Omote N, Sakamoto K, Li Q, Schupp JC, Adams T, Ahangari F, Chioccioli M, DeIuliis G, Hashimoto N, Hasegawa Y, Kaminski N. Long noncoding RNA TINCR is a novel regulator of human bronchial epithelial cell differentiation state. Physiological Reports 2021, 9: e14727. PMID: 33527707, PMCID: PMC7851438, DOI: 10.14814/phy2.14727.Peer-Reviewed Original ResearchConceptsTerminal differentiation-induced lncRNANormal human bronchial epithelial cellsTINCR overexpressionCell differentiationNotch genesTissue developmentBronchial epithelial cellsExtracellular matrix organizationCell phenotypeRNA sequencing analysisNumerous biological functionsRole of lncRNAsCell differentiation stateEpithelial cellsHuman bronchial epithelial cellsCiliated cell differentiationStaufen1 proteinNovel regulatorBasal cell phenotypeDownstream regulatorsRNA immunoprecipitationBiological functionsCritical regulatorDifferential expressionDifferentiation stateErythroid enucleation: a gateway into a “bloody” world
Menon V, Ghaffari S. Erythroid enucleation: a gateway into a “bloody” world. Experimental Hematology 2021, 95: 13-22. PMID: 33440185, PMCID: PMC8147720, DOI: 10.1016/j.exphem.2021.01.001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBirdsCalciumCell NucleusChromatinColony-Forming Units AssayComputational BiologyCytokinesCytoskeletal ProteinsDNA-Binding ProteinsErythroblastsErythrocytesErythropoiesisIntercellular Signaling Peptides and ProteinsMammalsMiceMicroRNAsProto-Oncogene ProteinsReceptors, Thyroid HormoneRepressor ProteinsReticulocytesrho GTP-Binding ProteinsTranscription FactorsTransport VesiclesYolk SacConceptsTerminal erythroid maturationFormation of reticulocytesEnucleation processHematopoietic stem cellsTranscription factorsCytoskeletal proteinsErythroid maturationFascinating processOrthochromatic erythroblastsTerminal maturationRate-limiting stepStem cellsIntricate processMaturationRed blood cellsCellsRBC productionMicroRNAsProteinProduction ex vivoErythroblastsEx vivoMechanismDaily productionProduction
2020
Microcephalin 1/BRIT1-TRF2 interaction promotes telomere replication and repair, linking telomere dysfunction to primary microcephaly
Cicconi A, Rai R, Xiong X, Broton C, Al-Hiyasat A, Hu C, Dong S, Sun W, Garbarino J, Bindra RS, Schildkraut C, Chen Y, Chang S. Microcephalin 1/BRIT1-TRF2 interaction promotes telomere replication and repair, linking telomere dysfunction to primary microcephaly. Nature Communications 2020, 11: 5861. PMID: 33203878, PMCID: PMC7672075, DOI: 10.1038/s41467-020-19674-0.Peer-Reviewed Original ResearchAminopeptidasesAnimalsBinding SitesCalorimetryCell Cycle ProteinsCytoskeletal ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDNA DamageFibroblastsHeLa CellsHistonesHumansMiceMicrocephalyMutationProtein Interaction Domains and MotifsSerine ProteasesShelterin ComplexTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding
Kadry YA, Maisuria EM, Huet-Calderwood C, Calderwood DA. Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding. Journal Of Biological Chemistry 2020, 295: 11161-11173. PMID: 32546480, PMCID: PMC7415974, DOI: 10.1074/jbc.ra120.013618.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsCricetulusCytoskeletal ProteinsFocal AdhesionsHEK293 CellsHumansIntegrinsProtein BindingProtein DomainsConceptsKindlin-3Kindlin-2Focal adhesionsIntegrin cytoplasmic domainTransmembrane adhesion receptorsComparative sequence analysisLive-cell imagingAbility of cellsCytoplasmic domainF3 subdomainsMammalian cellsCytoplasmic componentsExtracellular environmentAdhesion receptorsKindlinSequence analysisIntegrin familySelf-associationIntegrin bindingPhysiological importanceMolecular levelPoint mutationsProteinCellsAdhesionShootin‐1 is required for nervous system development in zebrafish
Emerson S, Stergas H, Bupp‐Chickering S, Ebert A. Shootin‐1 is required for nervous system development in zebrafish. Developmental Dynamics 2020, 249: 1285-1295. PMID: 32406957, DOI: 10.1002/dvdy.194.Peer-Reviewed Original ResearchConceptsNervous system developmentLoss of repressionShootin-1Peripheral nervous systemRepulsive axon guidance cuesDownstream signaling mechanismsPhenotypic consequencesNervous systemAxon guidance cuesNeuronal polarityPatterning defectsMicroarray screeningRetinal pigment epitheliumCell migrationGuidance cuesSignaling mechanismsFunctional roleImpaired migrationPLXNA2RepressionPigment epitheliumOptic vesiclePathfinding errorsZebrafishRegulationCrystal Structure of Keratin 1/10(C401A) 2B Heterodimer Demonstrates a Proclivity for the C-Terminus of Helix 2B to Form Higher Order Molecular Contacts.
Lomakin IB, Hinbest AJ, Ho M, Eldirany SA, Bunick CG. Crystal Structure of Keratin 1/10(C401A) 2B Heterodimer Demonstrates a Proclivity for the C-Terminus of Helix 2B to Form Higher Order Molecular Contacts. The Yale Journal Of Biology And Medicine 2020, 93: 3-17. PMID: 32226330, PMCID: PMC7087056.Peer-Reviewed Original ResearchDirectional allosteric regulation of protein filament length
Jermyn AS, Cao W, Elam WA, De La Cruz EM, Lin MM. Directional allosteric regulation of protein filament length. Physical Review E 2020, 101: 032409. PMID: 32290018, PMCID: PMC7758089, DOI: 10.1103/physreve.101.032409.Peer-Reviewed Original Research
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