2014
Two Amino Acid Residues Confer Different Binding Affinities of Abelson Family Kinase Src Homology 2 Domains for Phosphorylated Cortactin*
Gifford SM, Liu W, Mader CC, Halo TL, Machida K, Boggon TJ, Koleske AJ. Two Amino Acid Residues Confer Different Binding Affinities of Abelson Family Kinase Src Homology 2 Domains for Phosphorylated Cortactin*. Journal Of Biological Chemistry 2014, 289: 19704-19713. PMID: 24891505, PMCID: PMC4094080, DOI: 10.1074/jbc.m114.556480.Peer-Reviewed Original ResearchConceptsAbl SH2 domainSH2 domainAbl family kinasesFamily kinasesSrc homology 2 domainCell edge protrusionAbl SH2Similar N-terminal sequencesImportant non-redundant rolesWild-type levelsAmino acid sequenceAmino acid positionsN-terminal sequenceNon-redundant roleCell morphogenesisArg substrateCellular functionsSpecific phosphotyrosineCell peripheryAcid sequenceSerine 187Edge protrusionTarget proteinsType levelsDifferent binding affinities
2010
The Abl and Arg non‐receptor tyrosine kinases regulate different zones of stress fiber, focal adhesion, and contractile network localization in spreading fibroblasts
Peacock JG, Couch BA, Koleske AJ. The Abl and Arg non‐receptor tyrosine kinases regulate different zones of stress fiber, focal adhesion, and contractile network localization in spreading fibroblasts. Cytoskeleton 2010, 67: 666-675. PMID: 20737438, PMCID: PMC2955401, DOI: 10.1002/cm.20479.Peer-Reviewed Original ResearchConceptsCell peripheryPhosphorylated myosin light chainFocal adhesionsActomyosin contractilitySpatial regulationFocal adhesion dynamicsNon-receptor tyrosine kinaseAbl functionAdhesion dynamicsMutant cellsAbl familyFA formationStress fibersEdge protrusionMyosin light chainF-actinTyrosine kinaseRhoA activityInhibitory complexWT cellsArg functionAdhesive structuresCell migrationAdhesion elementsP120
2008
Retroviruses Human Immunodeficiency Virus and Murine Leukemia Virus Are Enriched in Phosphoinositides
Chan R, Uchil PD, Jin J, Shui G, Ott DE, Mothes W, Wenk MR. Retroviruses Human Immunodeficiency Virus and Murine Leukemia Virus Are Enriched in Phosphoinositides. Journal Of Virology 2008, 82: 11228-11238. PMID: 18799574, PMCID: PMC2573248, DOI: 10.1128/jvi.00981-08.Peer-Reviewed Original ResearchConceptsPlasma membraneMurine leukemia virusHIV-1 buddingLipid contentLeukemia virusMass spectrometry analysisCholesterol-rich regionsOverall lipid contentCell peripheryMutant virionsLipid envelopeTotal lipid contentPhosphorylated derivativesSpectrometry analysisPhosphoinositideRetrovirusesMembraneCellsMatrix domainParticle releaseHuman immunodeficiency virus type 1Immunodeficiency virus type 1VirusVirus type 1Phosphatidylinositol
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
Integrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane
Bradley WD, Hernández SE, Settleman J, Koleske AJ. Integrin Signaling through Arg Activates p190RhoGAP by Promoting Its Binding to p120RasGAP and Recruitment to the Membrane. Molecular Biology Of The Cell 2006, 17: 4827-4836. PMID: 16971514, PMCID: PMC1635390, DOI: 10.1091/mbc.e06-02-0132.Peer-Reviewed Original ResearchConceptsCell peripheryP120 bindingGene Tyrosine KinaseRho family GTPases RhoAActin stress fibersIntegrin-mediated adhesionWild-type fibroblastsP190 phosphorylationFocal adhesionsGTPases RhoARho activityStress fibersEssential effectorTyrosine kinaseAdhesive environmentCell attachmentP190P120P190RhoGAPP120RasGAPPhosphorylationComplex formationBindingRecruitmentRho
2004
The Abl-related gene (Arg) requires its F-actin–microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion
Miller AL, Wang Y, Mooseker MS, Koleske AJ. The Abl-related gene (Arg) requires its F-actin–microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion. Journal Of Cell Biology 2004, 165: 407-420. PMID: 15138293, PMCID: PMC2172189, DOI: 10.1083/jcb.200308055.Peer-Reviewed Original ResearchConceptsLamellipodial dynamicsCross-linking activityF-actin-binding domainFluorescent protein fusionsMT-binding domainNonreceptor tyrosine kinaseFilamentous actin bundlesWild-type fibroblastsCell polarityProtein fusionsMembrane protrusionsCell peripheryLamellipodial protrusionCell protrusionsActin bundlesMolecular mechanismsTyrosine kinaseF-actinMicrotubulesArgFibroblast adhesionABLHigh affinityFibroblastsProtrusion
2003
Nanometer targeting of microtubules to focal adhesions
Krylyshkina O, Anderson KI, Kaverina I, Upmann I, Manstein DJ, Small JV, Toomre DK. Nanometer targeting of microtubules to focal adhesions. Journal Of Cell Biology 2003, 161: 853-859. PMID: 12782685, PMCID: PMC2172972, DOI: 10.1083/jcb.200301102.Peer-Reviewed Original ResearchConceptsTotal internal reflection fluorescence microscopyAdhesion complexesIntact microtubule cytoskeletonReflection fluorescence microscopyGFP-CLIP-170Substrate adhesionFocal adhesionsMicrotubule cytoskeletonCell movementCell peripheryCommon cytoskeletal elementsMicrotubule tipsAdhesion fociCytoskeletal elementsPolymerizing microtubulesTip complexGFP-tubulinMicrotubule endsFluorescence microscopyMicrotubulesMultiple microtubulesSite targetingCentral roleComplexesTargeting
2000
Hematopoietic reconstitution of SLP-76 corrects hemostasis and platelet signaling through αIIbβ3 and collagen receptors
Judd B, Myung P, Leng L, Obergfell A, Pear W, Shattil S, Koretzky G. Hematopoietic reconstitution of SLP-76 corrects hemostasis and platelet signaling through αIIbβ3 and collagen receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 12056-12061. PMID: 11050236, PMCID: PMC17293, DOI: 10.1073/pnas.97.22.12056.Peer-Reviewed Original ResearchConceptsSLP-76Alpha IIbAdapter protein SLP-76SLP-76 functionSLP-76-deficient miceRapid tyrosine phosphorylationSLP-76-deficient plateletsTyrosine phosphorylated proteinsCollagen receptorCollagen receptor signalingT cell developmentPlatelet fibrinogen receptorPhosphorylated proteinsActin rearrangementCell peripheryLamellipodial extensionTyrosine phosphorylationCell developmentMurine plateletsRetroviral transductionReceptor signalingBind fibrinogenHematopoietic cellsFibrinogen receptorPlatelet-bound fibrinogenCompartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast
Barral Y, Mermall V, Mooseker M, Snyder M. Compartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast. Molecular Cell 2000, 5: 841-851. PMID: 10882120, DOI: 10.1016/s1097-2765(00)80324-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsCarrier ProteinsCell CompartmentationCell Cycle ProteinsCell DivisionCell MembraneCell PolarityCytoplasmCytoskeletal ProteinsExocytosisFungal ProteinsMorphogenesisMyosin Heavy ChainsMyosin Type IIMyosin Type VProtein-Tyrosine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsConceptsCell polaritySpecialized plasma membrane domainsIsotropic bud growthPlasma membrane domainsBud neckMembrane domainsMother cellsCell cortexCell peripheryGrowth polaritySeptinsProper regulationBud surfaceBiological processesBud growthCell polarizationIsotropic growthCortical domainsExocytosisPatch stabilityActive siteCellsMyo2Sec5SPA2
1999
The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*
Rosenthal J, Chen H, Slepnev V, Pellegrini L, Salcini A, Di Fiore P, De Camilli P. The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*. Journal Of Biological Chemistry 1999, 274: 33959-33965. PMID: 10567358, DOI: 10.1074/jbc.274.48.33959.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCoated VesiclesCricetinaeDNA, ComplementaryFluorescent Antibody TechniqueGene ExpressionHumansIntracellular Signaling Peptides and ProteinsLuciferasesMaleMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsPhylogenyProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue DistributionVesicular Transport ProteinsConceptsEpsin 1Clathrin coatClathrin adaptor AP-2New protein modulesNew protein familyTerminal regionAdaptor AP-2Family of proteinsRat brain libraryNPF motifsProtein modulesProtein familyCell peripheryAP-2Membrane dynamicsSimilar proteinsBrain libraryClathrinEps15Vesicle fractionEpsinGreen fluorescentGolgi regionCell surfaceProtein
1998
Protein-tyrosine Phosphatase Shp-2 Regulates Cell Spreading, Migration, and Focal Adhesion*
Yu D, Qu C, Henegariu O, Lu X, Feng G. Protein-tyrosine Phosphatase Shp-2 Regulates Cell Spreading, Migration, and Focal Adhesion*. Journal Of Biological Chemistry 1998, 273: 21125-21131. PMID: 9694867, DOI: 10.1074/jbc.273.33.21125.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell AdhesionCell Adhesion MoleculesCell LineCell MovementCytoskeletal ProteinsFibroblastsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHeterozygoteHomozygoteIntracellular Signaling Peptides and ProteinsMicePaxillinPhenotypePhosphoproteinsProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProtein-Tyrosine KinasesSH2 Domain-Containing Protein Tyrosine PhosphatasesConceptsShp-2 mutant cellsMutant cellsFocal adhesionsSHP-2Tyrosine phosphataseProtein tyrosine phosphatase SHP-2SHP-2 tyrosine phosphataseCell spreadingFunctional SHP-2SHP-2 mutationsPhosphatase SHP-2Cytoplasmic tyrosine phosphataseF-actin aggregationWild-type cellsFocal adhesion kinaseMesodermal patterningSH2 domainFAK dephosphorylationCytoskeletal architectureSrc SH2Adhesion kinaseSignal relayCell peripheryGrowth factor receptorCell motility
1996
Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
Wirth J, Jensen K, Post P, Bement W, Mooseker M. Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. Journal Of Cell Science 1996, 109: 653-661. PMID: 8907710, DOI: 10.1242/jcs.109.3.653.Peer-Reviewed Original ResearchConceptsProtein domainsHL-60 cellsRho/Rac familyNovel N-terminal domainGTPase-activating protein (GAP) domainUnconventional myosin heavy chainRas-like G proteinsPrimary structurePutative actin-binding siteAmino acidsFull-length primary structureSkeletal muscle myosin IIN-terminal domainAmino acid extensionActin-binding siteProtein kinase CNorthern blot analysisMuscle myosin IIRac familyDifferent human tissuesUndifferentiated HL-60 cellsRegulatory domainPutative zincRac GTPaseCell periphery
1995
Hydrogen peroxide-induced endothelial retraction is accompanied by a loss of the normal spatial organization of endothelial cell adhesion molecules.
Bradley JR, Thiru S, Pober JS. Hydrogen peroxide-induced endothelial retraction is accompanied by a loss of the normal spatial organization of endothelial cell adhesion molecules. American Journal Of Pathology 1995, 147: 627-41. PMID: 7677177, PMCID: PMC1870992.Peer-Reviewed Original ResearchConceptsMembrane protein distributionFocal adhesion plaquesAdjacent cellsNormal spatial organizationNew protein synthesisEndothelial cellsSurface protein expressionBeta 3 integrinActin organizationDendrite-like processesCell peripheryEndothelial retractionCell adhesion moleculeHuman umbilical vein endothelial cellsAdhesion plaquesUmbilical vein endothelial cellsCellular metabolismActin filamentsProtein distributionProtein synthesisVein endothelial cellsNormal endothelial cell functionEndothelial cell functionApical capCell retraction
1982
An electronmicroscopic study of microtubules in the development of marginal cells of the mouse stria vascularis
Santos-Sacchi J. An electronmicroscopic study of microtubules in the development of marginal cells of the mouse stria vascularis. Hearing Research 1982, 6: 7-13. PMID: 7054137, DOI: 10.1016/0378-5955(82)90003-x.Peer-Reviewed Original ResearchConceptsMouse stria vascularisPlasma membraneCellular extensionsNumerous cellular processesMarginal cellsSheet-like extensionsCellular processesCell peripheryLength of microtubulesGolgi bodiesDepolymerization of microtubulesCytoplasmic microtubulesMicrotubulesNumerous microtubulesCell processesOrganellesMitochondriaStria vascularisCellsMembraneAdult miceCytoplasmVesiclesPlasmalemmaMicrotubles
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