2017
Phosphorylated cortactin recruits Vav2 guanine nucleotide exchange factor to activate Rac3 and promote invadopodial function in invasive breast cancer cells
Rosenberg BJ, Gil-Henn H, Mader CC, Halo T, Yin T, Condeelis J, Machida K, Wu YI, Koleske AJ. Phosphorylated cortactin recruits Vav2 guanine nucleotide exchange factor to activate Rac3 and promote invadopodial function in invasive breast cancer cells. Molecular Biology Of The Cell 2017, 28: 1347-1360. PMID: 28356423, PMCID: PMC5426849, DOI: 10.1091/mbc.e16-12-0885.Peer-Reviewed Original ResearchConceptsInvasive breast cancer cellsInvadopodium maturationBreast cancer cellsActin nucleation-promoting factorCancer cellsSH2 domain bindsHuman SH2 domainsMatrix degradationNucleation-promoting factorsGuanine nucleotide exchange factor Vav2Actin-rich protrusionsSubsequent cell invasionExchange factor Vav2Active Rac3Invasive MDA-MB-231 breast cancer cellsMDA-MB-231 breast cancer cellsInvadopodial functionSH2 domainDomain bindsExchange factorKinase cascadeCortactin phosphorylationActin polymerizationMutant formsInvadopodia
2006
Shigella IpgB1 promotes bacterial entry through the ELMO–Dock180 machinery
Handa Y, Suzuki M, Ohya K, Iwai H, Ishijima N, Koleske AJ, Fukui Y, Sasakawa C. Shigella IpgB1 promotes bacterial entry through the ELMO–Dock180 machinery. Nature Cell Biology 2006, 9: 121-128. PMID: 17173036, DOI: 10.1038/ncb1526.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBacterial AdhesionCell LineCell MembraneDogsHeLa CellsHumansImmunoprecipitationMiceModels, BiologicalNIH 3T3 CellsProtein TransportRac GTP-Binding ProteinsRac1 GTP-Binding ProteinRNA InterferenceShigellaSignal TransductionTransduction, GeneticTransfectionConceptsMembrane rufflesCell motility proteinsRole of RhoGEpithelial cellsType III secretionWild-type cellsMembrane associationMotility proteinsPulldown assaysBinding partnerDock180 pathwayBacterial entryRufflesRac1 activityIpgB1EffectorsPivotal roleCellsELMODock180RhoGSpecial mechanismShigellaMachineryEngulfment
2004
Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation
Sini P, Cannas A, Koleske AJ, Di Fiore PP, Scita G. Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation. Nature Cell Biology 2004, 6: 268-274. PMID: 15039778, DOI: 10.1038/ncb1096.Peer-Reviewed Original ResearchConceptsGuanine nucleotide exchange factorsSos-1Rac activationTyrosine phosphorylationFunction of RacNon-receptor tyrosine kinase AblActin cytoskeleton remodellingNucleotide exchange factorsRac-GEF activityTyrosine kinase AblActivation of RTKsActivity of RacReceptor tyrosine kinasesCytoskeleton remodellingActin remodellingSignal transductionMolecular connectionMolecular mechanismsTyrosine kinaseBcr-Abl oncoproteinRacPharmacological interferencePhosphorylationGrowth factorABL signals