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
2015
Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase
Hudson AM, Mannix KM, Cooley L. Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase. Genetics 2015, 201: 1117-1131. PMID: 26384358, PMCID: PMC4649639, DOI: 10.1534/genetics.115.181289.Peer-Reviewed Original ResearchConceptsKelch functionE3 ligaseCullin-RING E3 ligaseGermline ring canalsActin cytoskeletal organizationDrosophila kelch proteinUbiquitin ligase activityCross-link F-actinUbiquitin E3 ligaseRing canalsKelch proteinProtein substratesCytoskeletal defectsCytoskeletal organizationCytoskeletal remodelingLigase activityCullin 3KelchF-actinCytoskeletonLigaseProteasomeVivoCul3Mutagenesis
2002
SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila
Zallen JA, Cohen Y, Hudson AM, Cooley L, Wieschaus E, Schejter ED. SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila. Journal Of Cell Biology 2002, 156: 689-701. PMID: 11854309, PMCID: PMC2174092, DOI: 10.1083/jcb.200109057.Peer-Reviewed Original ResearchMeSH KeywordsActin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceAnimalsAxonsBase SequenceBlastodermBrainCytoplasmCytoskeletal ProteinsDNA, ComplementaryDrosophilaDrosophila ProteinsGenes, InsectHumansInsect ProteinsMicrofilament ProteinsMolecular Sequence DataMorphogenesisMutagenesisOogenesisOvumProteinsSequence Homology, Amino AcidWiskott-Aldrich Syndrome ProteinConceptsWiskott-Aldrich syndrome proteinArp2/3 complexAdult eye morphologyScar/WAVECell fate decisionsActin-rich structuresCell biological eventsCortical filamentous actinCell morphologyDrosophila developmentMultiple cell typesNormal cell morphologySCAR homologueFate decisionsSyndrome proteinActin structuresFilamentous actinActin polymerizationCell shapeMorphological eventsCytoplasmic organizationEye morphologyBiological eventsCell typesDevelopmental requirements
1996
Single Amino Acid Mutations in Drosophila Fascin Disrupt Actin Bundling Function in Vivo
Cant K, Cooley L. Single Amino Acid Mutations in Drosophila Fascin Disrupt Actin Bundling Function in Vivo. Genetics 1996, 143: 249-258. PMID: 8722779, PMCID: PMC1207258, DOI: 10.1093/genetics/143.1.249.Peer-Reviewed Original ResearchConceptsEMS mutagenesis screenMutagenesis screenCytoplasm transportActin-bundling functionDiverse cellular processesIntragenic suppressor mutationsBundles actin filamentsCytoplasmic actin bundlesSingle amino acid mutationSerine 289Glutamic acid resultsAmino acid mutationsDominant suppressorsFascin functionFemale sterileSuppressor mutationsCellular processesC-terminusActin bundlesCentral domainActin filamentsSevere defectsMicrovillar projectionsAcid mutationsFilopodial extensions