2023
Abl2 repairs microtubules and phase separates with tubulin to promote microtubule nucleation
Duan D, Lyu W, Chai P, Ma S, Wu K, Wu C, Xiong Y, Sestan N, Zhang K, Koleske A. Abl2 repairs microtubules and phase separates with tubulin to promote microtubule nucleation. Current Biology 2023, 33: 4582-4598.e10. PMID: 37858340, PMCID: PMC10877310, DOI: 10.1016/j.cub.2023.09.018.Peer-Reviewed Original ResearchConceptsCOS-7 cellsMT nucleationMT latticeFamily kinasesTubulin recruitmentLiquid-liquid phase separationTubulin C-terminal tailsCryo-EM analysisC-terminal tailAbl family kinasesWild-type cellsC-terminal halfRescue frequencyGenetic experimentsNeuronal morphogenesisMicrotubule nucleationSplice isoformsMicrotubule dynamicsNocodazole treatmentMolecular mechanismsAxon guidanceCell migrationDamage sitesABL2MT assembly
2019
Regulation of MT dynamics via direct binding of an Abl family kinase
Hu Y, Lyu W, Lowery LA, Koleske AJ. Regulation of MT dynamics via direct binding of an Abl family kinase. Journal Of Cell Biology 2019, 218: 3986-3997. PMID: 31699690, PMCID: PMC6891085, DOI: 10.1083/jcb.201812144.Peer-Reviewed Original ResearchConceptsAbl family kinasesC-terminal halfFamily kinasesMT dynamicsMT growthTubulin C-terminal tailsC-terminal tailStable reexpressionEssential regulatorCell shapeBinds microtubulesMT polymerizationAbl kinaseGenetic studiesDirect bindingFunctional interactionKinaseMicrotubulesABL2ReexpressionMT behaviorBindingRegulatorProteinGrowthThe Functionally Important N‑Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation
Chatterjee M, Pollard TD. The Functionally Important N‑Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. Biochemistry 2019, 58: 3031-3041. PMID: 31243991, PMCID: PMC7336169, DOI: 10.1021/acs.biochem.9b00217.Peer-Reviewed Original ResearchConceptsN-terminal halfFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeC-terminal halfFull-length proteinSchizosaccharomyces pombeStructure prediction toolsPH domainScaffold proteinInsect cellsAnimal cellsContractile ringMyosin IIOrganizing centerAnillinMid1pProteinHydrodynamic measurementsPombeCytokinesisUndergoes phase separationCellsFungalPrediction tools
2018
Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension
Zhang K, Lyu W, Yu J, Koleske AJ. Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension. Molecular Biology Of The Cell 2018, 29: 2863-2873. PMID: 30256707, PMCID: PMC6249870, DOI: 10.1091/mbc.e18-01-0044.Peer-Reviewed Original ResearchConceptsCytoskeletal interactionsLamellipodium extensionTotal internal reflection fluorescence microscopyActin-rich structuresActin wavesActin-rich protrusionsN-terminal halfC-terminal halfNonreceptor tyrosine kinaseReflection fluorescence microscopyFoci colocalizeComplementation analysisLamellipodia protrusionKnockout cellsLamellipodium tipActin filament stabilizerCell shapeBind actinTyrosine kinaseCortactinABL2Fluorescence microscopyIntegrin β3High spatiotemporal resolutionPaxillinUsing disruptive insertional mutagenesis to identify the in situ structure‐function landscape of the Shigella translocator protein IpaB
Barta ML, Tachiyama S, Muthuramalingam M, Arizmendi O, Villanueva CE, Ramyar KX, Geisbrecht BV, Lovell S, Battaile KP, Picking WL, Picking WD. Using disruptive insertional mutagenesis to identify the in situ structure‐function landscape of the Shigella translocator protein IpaB. Protein Science 2018, 27: 1392-1406. PMID: 29672980, PMCID: PMC6153406, DOI: 10.1002/pro.3428.Peer-Reviewed Original ResearchConceptsTip complexInsertional mutagenesisTranslocator protein IpaBBacterial type III secretion systemType III secretion systemC-terminal halfN-terminal halfInsertion mutantsT3SS apparatusCellular functionsLatter mutantSecretion inductionMammalian cellsSecretion systemTC functionHost membraneBasal bodiesBacteriophage T4 lysozymeTertiary structureImpaired interactionIpaBPore formationT4 lysozymeBacterial surfaceMutants
2017
La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region
Philippe L, Vasseur JJ, Debart F, Thoreen CC. La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region. Nucleic Acids Research 2017, 46: gkx1237-. PMID: 29244122, PMCID: PMC5814973, DOI: 10.1093/nar/gkx1237.Peer-Reviewed Original ResearchMeSH KeywordsAutoantigensBase SequenceBinding SitesBinding, CompetitiveCell-Free SystemComputational BiologyEukaryotic Initiation Factor-4FGene Expression RegulationHEK293 CellsHumansMechanistic Target of Rapamycin Complex 1Models, GeneticPolyribosomesProtein BindingProtein BiosynthesisProtein Interaction Domains and MotifsPyrimidinesRibonucleoproteinsRNA, MessengerConceptsTOP mRNA translationAdjacent regulatory regionsMRNA translationCap-binding domainCap structureRegulatory regionsEukaryotic initiation factor 4FMRNA 5' cap structureIntrinsic repressive activityTerminal oligopyrimidine motifsInitiation factor 4FMRNA 5' endsC-terminal halfGrowth-related mRNAsTOP mRNAsRepressive activityTranslation factorsMRNA targetsCoordinated changesGene expressionLARP1Cell growthProtein 1Top sequenceMRNA
2007
The Abl-related Gene Tyrosine Kinase Acts through p190RhoGAP to Inhibit Actomyosin Contractility and Regulate Focal Adhesion Dynamics upon Adhesion to Fibronectin
Peacock JG, Miller AL, Bradley WD, Rodriguez OC, Webb DJ, Koleske AJ. The Abl-related Gene Tyrosine Kinase Acts through p190RhoGAP to Inhibit Actomyosin Contractility and Regulate Focal Adhesion Dynamics upon Adhesion to Fibronectin. Molecular Biology Of The Cell 2007, 18: 3860-3872. PMID: 17652459, PMCID: PMC1995720, DOI: 10.1091/mbc.e07-01-0075.Peer-Reviewed Original ResearchConceptsFocal adhesion dynamicsFocal adhesionsActomyosin contractilityAdhesion dynamicsActin-dependent protrusionsGene Tyrosine KinaseCell migrationCell body translocationAbl family kinasesWild-type cellsC-terminal halfDistinct functional domainsN-terminal halfF-actin stress fibersStress fiber formationInhibits cell migrationKinase inhibitsFamily kinasesCell peripheryStress fibersActin polymerizationFunctional domainsKinase activityTyrosine kinaseWT cells
2006
The rab Exchange Factor Sec2p Reversibly Associates with the Exocyst
Medkova M, France Y, Coleman J, Novick P. The rab Exchange Factor Sec2p Reversibly Associates with the Exocyst. Molecular Biology Of The Cell 2006, 17: 2757-2769. PMID: 16611746, PMCID: PMC1474791, DOI: 10.1091/mbc.e05-10-0917.Peer-Reviewed Original ResearchConceptsSecretory vesiclesExchange factor Sec2pTemperature-sensitive growthC-terminal halfExocyst complexExocytic sitesRab GTPaseExchange factorMutant resultsMutant correlatesRecycling pathwaySec2pExocystNucleotide exchangePlasma membraneSec4pSec15pVesiclesMislocalizationEffectorsPolarized transportAssociatesGTPaseExocytosisPathway
2004
How do Abl family kinases regulate cell shape and movement?
Hernández SE, Krishnaswami M, Miller AL, Koleske AJ. How do Abl family kinases regulate cell shape and movement? Trends In Cell Biology 2004, 14: 36-44. PMID: 14729179, DOI: 10.1016/j.tcb.2003.11.003.Peer-Reviewed Original ResearchConceptsAbl family kinasesFamily kinasesAdhesion receptorsC-terminal halfCytoskeletal regulatory proteinsNonreceptor tyrosine kinaseCell morphogenesisCytoskeletal dynamicsRecent biochemicalCytoskeletal rearrangementsCytoskeletal structuresCytoskeletal componentsRegulatory proteinsCell shapeGenetic analysisTyrosine kinaseKinaseCell surfaceARG proteinRelay signalsProteinLeukemia cellsDrosophilaCrystallographic analysisMorphogenesis
1997
Glutamyl-tRNA sythetase.
Freist W, Gauss D, Söll D, Lapointe J. Glutamyl-tRNA sythetase. Biological Chemistry 1997, 378: 1313-29. PMID: 9426192.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesNegative eubacteriaBacterial glutamyl-tRNA synthetasesATP/PPiHigh molecular mass complexesClass I aminoacyl-tRNA synthetasesCytoplasm of eukaryotesE. coli GlnRSGlutamyl-tRNA synthetasesMolecular mass complexesN-terminal halfC-terminal halfAmino acid residuesDihydrouridine (DHU) armPhylogenetic studiesSpecific amidotransferaseGlutamyl-prolylMass complexesTRNA synthetasesCognate tRNAAcid residuesAcceptor stemSynthetasesDefinition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2.
McMahan CJ, Sadofsky MJ, Schatz DG. Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2. The Journal Of Immunology 1997, 158: 2202-10. PMID: 9036966, DOI: 10.4049/jimmunol.158.5.2202.Peer-Reviewed Original Research
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