2020
HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis
Gerdes JA, Mannix KM, Hudson AM, Cooley L. HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis. Genetics 2020, 216: 717-734. PMID: 32883702, PMCID: PMC7648574, DOI: 10.1534/genetics.120.303629.Peer-Reviewed Original ResearchConceptsGermline ring canalsRing canalsActin cytoskeletonF-actinDrosophila melanogaster oogenesisSomatic follicle cellsCombination of CRISPRF-actin accumulationF-actin recruitmentFilamentous actin cytoskeletonFemale germlineActin structuresFruit flyHigh fecundityFollicle cellsCytoskeletonGermlineOverexpressionAccumulationDrosophilaOogenesisMutagenesisCRISPRFilaminGenes
2003
Drosophila filamin is required for follicle cell motility during oogenesis
Sokol NS, Cooley L. Drosophila filamin is required for follicle cell motility during oogenesis. Developmental Biology 2003, 260: 260-272. PMID: 12885568, DOI: 10.1016/s0012-1606(03)00248-3.Peer-Reviewed Original ResearchConceptsGermline cystsFilamin proteinsCell motilityFollicle cell morphogenesisActin-binding domainActin binding proteinsFilamin repeatsDrosophila ovaryFilamin functionCell morphogenesisDrosophila filaminFilamin familyCell movementProtein 120Cell shapeBorder cellsCell locomotionFollicle cellsBinding proteinPoint mutationsInitial encapsulationProteinMorphogenesisReduced expressionFilamin
2001
Filamins as integrators of cell mechanics and signalling
Stossel T, Condeelis J, Cooley L, Hartwig J, Noegel A, Schleicher M, Shapiro S. Filamins as integrators of cell mechanics and signalling. Nature Reviews Molecular Cell Biology 2001, 2: 138-145. PMID: 11252955, DOI: 10.1038/35052082.Peer-Reviewed Original ResearchConceptsFilamin geneAmino-terminal actin-binding domainActin filamentsDiverse cellular proteinsActin-binding domainDrosophila filaminCellular proteinsX chromosomeCarboxyl terminusHuman filaminChromosome 3Dictyostelium amoebaeChromosome 7FilaminMembrane receptorsCell mechanicsGenesPeripheral cytoplasmActin gelsSubunitsMutationsFilamentsPeriventricular heterotopiaCell structureDrosophila
2000
Physical and genetic interaction of filamin with presenilin in Drosophila
Guo Y, Zhang S, Sokol N, Cooley L, Boulianne G. Physical and genetic interaction of filamin with presenilin in Drosophila. Journal Of Cell Science 2000, 113: 3499-3508. PMID: 10984440, DOI: 10.1242/jcs.113.19.3499.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAlzheimer DiseaseAmino Acid SequenceAnimalsBlotting, WesternCarrier ProteinsCloning, MolecularContractile ProteinsDrosophila melanogasterEmbryo, NonmammalianFemaleFilaminsGene Expression Regulation, DevelopmentalHumansInsect ProteinsLarvaMaleMembrane ProteinsMicrofilament ProteinsMolecular Sequence DataPresenilin-1Presenilin-2Protein BindingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTwo-Hybrid System TechniquesConceptsN-terminal actin-binding domainOverall amino acid identityOverexpression of presenilinFamilial Alzheimer's diseaseTransmembrane domain proteinActin-binding domainAmino acid identityLarge hydrophilic loopDrosophila filaminDomain proteinsGenetic interactionsAlternative splicingHydrophilic loopAcid identityTerminal domainDrosophilaHuman filaminChromosome 3Spliced formsFilaminAdult phenotypeLoop regionPresenilinNovel familyLong form