2020
Crystal structure of a guanine nucleotide exchange factor encoded by the scrub typhus pathogen Orientia tsutsugamushi
Lim C, Berk JM, Blaise A, Bircher J, Koleske AJ, Hochstrasser M, Xiong Y. Crystal structure of a guanine nucleotide exchange factor encoded by the scrub typhus pathogen Orientia tsutsugamushi. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 30380-30390. PMID: 33184172, PMCID: PMC7720168, DOI: 10.1073/pnas.2018163117.Peer-Reviewed Original ResearchConceptsBacterial GEFStructure-guided mutational analysisExchange factor domainRho family GTPasesObvious sequence similarityRho GTPases Rac1Pathogen Orientia tsutsugamushiAlters cell morphologyInteraction screenConvergent evolutionGEF domainHost interactorsExchange factorNucleotide displacementGEF activityCellular processesSequence similarityCytoskeletal structuresGTPases Rac1Ectopic expressionMutational analysisGEFRac1Factor domainPathogenic bacterium
2018
Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion
Hudson AM, Mannix KM, Gerdes JA, Kottemann MC, Cooley L. Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion. Development 2018, 146: dev169219. PMID: 30559276, PMCID: PMC6340150, DOI: 10.1242/dev.169219.Peer-Reviewed Original ResearchConceptsTandem affinity purificationUbiquitin ligase complexCullin-3 functionShort sequence motifsSpecialized cytoskeletal structuresUbiquitin-proteasome systemF-actin cytoskeletonSpecialized actinLigase complexActin cytoskeletonRing canalsSequence motifsGenetic evidenceCytoskeletal structuresAffinity purificationCytoskeletonSubstrate degradationBiochemical evidenceUnusual mechanismKelchCRL3CullinMass spectrometryOogenesisMutagenesis
2017
A bifurcated signaling cascade of NIMA-related kinases controls distinct kinesins in anaphase
Cullati SN, Kabeche L, Kettenbach AN, Gerber SA. A bifurcated signaling cascade of NIMA-related kinases controls distinct kinesins in anaphase. Journal Of Cell Biology 2017, 216: 2339-2354. PMID: 28630147, PMCID: PMC5551695, DOI: 10.1083/jcb.201512055.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnaphaseChromatography, AffinityCytokinesisHeLa CellsHumansHydrolysisIntracellular Signaling Peptides and ProteinsKinesinsNIMA-Related KinasesOncogene ProteinsPhosphorylationProtein Serine-Threonine KinasesRNA InterferenceSignal TransductionSpindle ApparatusTandem Mass SpectrometryTime FactorsTransfectionConceptsProtein-protein interactionsAnaphase central spindleNEK kinasesKinase NEK6Distinct kinesinsBundling activityPosttranslational modificationsCentral spindleCytoskeletal structuresNek9MKlp2Genetic materialTimely localizationKinesinCytokinesisNEK6Sophisticated networkKinaseNIMANEK7KIF14CascadeAnaphaseLocalizationMidzone
2010
Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton
Hudson AM, Cooley L. Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton. Journal Of Cell Biology 2010, 188: 29-37. PMID: 20065088, PMCID: PMC2812842, DOI: 10.1083/jcb.200909017.Peer-Reviewed Original ResearchConceptsDrosophila KelchCullin 3Cullin-RING ubiquitin E3 ligasesGermline ring canalsSubstrate adaptor proteinCullin-RING ligaseDiverse protein familiesF-actin cytoskeletal structureUbiquitin E3 ligasesProtein ubiquitylationActin cytoskeletonE3 ligasesRing canalsAdaptor proteinProtein familySequence motifsCytoskeletal structuresFilamentous actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeats
2007
A Critical Role for Cortactin Phosphorylation by Abl-Family Kinases in PDGF-Induced Dorsal-Wave Formation
Boyle SN, Michaud GA, Schweitzer B, Predki PF, Koleske AJ. A Critical Role for Cortactin Phosphorylation by Abl-Family Kinases in PDGF-Induced Dorsal-Wave Formation. Current Biology 2007, 17: 445-451. PMID: 17306540, DOI: 10.1016/j.cub.2007.01.057.Peer-Reviewed Original ResearchConceptsAbl family kinasesCortactin phosphorylationActin regulatory protein cortactinTyrosine kinaseAbl family tyrosine kinasesSrc family kinasesNonreceptor tyrosine kinaseHuman protein microarrayCell morphogenesisActin reorganizationCytoskeletal rearrangementsProtein cortactinGrowth factor receptorLamellipodial protrusionCytoskeletal structuresCell motilityProper regulationPDGF treatmentTyrosine residuesCortactinKinaseNovel substrateDownstream actionsPhosphorylationProtein microarrays
2006
Regulation of Cytoskeletal Dynamics and Cell Morphogenesis by Abl Family Kinases
Koleske A. Regulation of Cytoskeletal Dynamics and Cell Morphogenesis by Abl Family Kinases. Molecular Biology Intelligence Unit 2006, 48-67. DOI: 10.1007/978-0-387-68744-5_5.Peer-Reviewed Original ResearchCell morphogenesisProtrusive structuresActin rich protrusive structuresFormation of actinAbl family kinasesNonreceptor tyrosine kinaseExtended C-terminusMetazoan organismsArp2/3 complexCytoskeletal dynamicsProtein complexesRac GTPasesExhibit defectsFamily kinasesNeuronal morphogenesisAbl familyCytoskeletal rearrangementsCytoskeletal networkCytoskeletal structuresEssential regulatorMutant animalsC-terminusActin filamentsTyrosine kinaseF-actin
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
2001
The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin
Wang Y, Miller A, Mooseker M, Koleske A. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14865-14870. PMID: 11752434, PMCID: PMC64950, DOI: 10.1073/pnas.251249298.Peer-Reviewed Original ResearchConceptsF-actin-binding domainActin-rich structuresAbl family kinasesNonreceptor tyrosine kinaseF-actinActin cytoskeletonFamily kinasesFluorescent protein fusion proteinTyrosine kinaseActin-bundling activityProtein fusion proteinActin cytoskeletal structuresCellular morphogenesisSwiss 3T3 fibroblastsBundling activityDeletion mutantsCytoskeletal structuresC-terminusFusion proteinFunctional interactionKinaseActin moleculesCytoskeletonPositive cooperativityArg
1999
Regulation of the small GTP‐binding protein Rho by cell adhesion and the cytoskeleton
Ren X, Kiosses W, Alexander Schwartz M. Regulation of the small GTP‐binding protein Rho by cell adhesion and the cytoskeleton. The EMBO Journal 1999, 18: 578-585. PMID: 9927417, PMCID: PMC1171150, DOI: 10.1093/emboj/18.3.578.Peer-Reviewed Original ResearchConceptsFocal adhesionsRho activationRho activityExtracellular matrixSmall GTPProtein RhoLysophosphatidic acidStress fibersCell adhesionRho-dependent mannerActin stress fibersHigh Rho activitySwiss 3T3 cellsNegative feedback loopAdherent cellsCytoskeletal structuresSoluble factorsCytochalasin DRhoGTPPresence of serumCellsActivationRegulationAdhesion
1998
Double-stranded RNA induces mRNA degradation in Trypanosoma brucei
Ngô H, Tschudi C, Gull K, Ullu E. Double-stranded RNA induces mRNA degradation in Trypanosoma brucei. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14687-14692. PMID: 9843950, PMCID: PMC24510, DOI: 10.1073/pnas.95.25.14687.Peer-Reviewed Original ResearchConceptsMRNA degradationUntranslated regionFlagellar attachment zoneMRNA 5' untranslated regionAlpha-tubulin synthesisImportant protozoan parasitesCaenorhabditis elegansAlpha-tubulin mRNACellular mRNAsTrypanosome cellsGenetic interferenceCytoskeletal structuresCleavage furrowDsRNA transfectionSame phenotypeCytokinesisComplex cortical structureFlagellar axonemeTubulin mRNAPlasmid vectorProtozoan parasiteVivo expressionAttachment zoneMRNADsRNA
1992
Novel form of growth cone motility involving site-directed actin filament assembly
Forscher P, Lin C, Thompson C. Novel form of growth cone motility involving site-directed actin filament assembly. Nature 1992, 357: 515-518. PMID: 1608453, DOI: 10.1038/357515a0.Peer-Reviewed Original ResearchConceptsActin filament assemblyFilament assemblyNeuronal growth conesCortical F-actin networkMembrane-cytoskeletal interfaceF-actin assemblyF-actin networkGrowth conesGrowth cone migrationGrowth cone motilityExtracellular signalsBacterial parasiteMembrane proteinsCell movementCytoskeletal structuresIntracellular movementDevelopmental processesBead movementCell locomotionCone migrationMorphogenic changesMotile cellsAxonal guidanceCone motilityCellular mechanisms
1986
Calcium and the Regulation of Cytoskeletal Assembly, Structure and Contractility
Mooseker M, Coleman T, Conzelman K. Calcium and the Regulation of Cytoskeletal Assembly, Structure and Contractility. Novartis Foundation Symposia 1986, 122: 232-249. PMID: 3792141, DOI: 10.1002/9780470513347.ch14.Peer-Reviewed Original ResearchConceptsActin-binding proteinsCytoskeletal assemblyActin filament interactionsCase of actinSubset of proteinsInteraction of actinActin assemblyCytoskeletal networkCytoskeletal structuresMode of Ca2Dependent regulationActin filamentsSpecific functionsProteinRegulationCentral roleActinFilament interactionAssemblyMyosin interactionCa2Functional classInteractionMembrane
1983
Regulation of Cytoskeletal Structure and Contractility in the Brush Border
Mooseker M, Keller T, Hirokawa N. Regulation of Cytoskeletal Structure and Contractility in the Brush Border. Novartis Foundation Symposia 1983, 95: 195-215. PMID: 6552204, DOI: 10.1002/9780470720769.ch12.Peer-Reviewed Original ResearchConceptsIntestinal epithelial cellsBrush borderEpithelial cellsRat brush bordersIsometric contractionFree Ca2ContractilityBrush border proteinsRegulation of forceContractionChicken intestineAnalysis of Ca2Light chainCa2Microvillar rootletsActin-severing proteinBrush border myosinPresence of Ca2Circumferential bundlesCalmodulin functionTerminal web regionCalciumCellsPhosphorylationCytoskeletal structures
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