2020
Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches
Pandit NG, Cao W, Bibeau J, Johnson-Chavarria EM, Taylor EW, Pollard TD, De La Cruz EM. Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 13519-13528. PMID: 32461373, PMCID: PMC7306818, DOI: 10.1073/pnas.1911183117.Peer-Reviewed Original ResearchConceptsActin filament branchesArp2/3 complexMother filamentFilament branchesTotal internal reflection fluorescence microscopyEssential cellular functionsMechanical forcesActin filament networkReflection fluorescence microscopyCellular functionsActin networkCell motilityComplex generatesActin filamentsArp2/3Filament networkFluorescence microscopyState 1Branch junctionsState 2FilamentsComplexesPhosphate releaseMuscle actinADP
2017
Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly
Zimmermann D, Homa KE, Hocky GM, Pollard LW, De La Cruz EM, Voth GA, Trybus KM, Kovar DR. Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly. Nature Communications 2017, 8: 703. PMID: 28951543, PMCID: PMC5614989, DOI: 10.1038/s41467-017-00445-3.Peer-Reviewed Original ResearchPhosphomimetic S3D cofilin binds but only weakly severs actin filaments
Elam WA, Cao W, Kang H, Huehn A, Hocky GM, Prochniewicz E, Schramm AC, Negrón K, Garcia J, Bonello TT, Gunning PW, Thomas DD, Voth GA, Sindelar CV, De La Cruz EM. Phosphomimetic S3D cofilin binds but only weakly severs actin filaments. Journal Of Biological Chemistry 2017, 292: 19565-19579. PMID: 28939776, PMCID: PMC5712599, DOI: 10.1074/jbc.m117.808378.Peer-Reviewed Original ResearchConceptsActin bindingWild-type cofilinActin filament severingHigh cooperativitySubstitution of serineCofilin bindsActin cytoskeletonProtein cofilinCell divisionSer-3Filament severingAtom molecular dynamics simulationsSubunit interactionsN-terminusCofilinBiological processesActin filamentsTime-resolved phosphorescence anisotropyElectron cryomicroscopyRapid remodelingPhosphorylationSeveringFilament mechanical propertiesActin segmentsFilaments
2011
Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries
Suarez C, Roland J, Boujemaa-Paterski R, Kang H, McCullough BR, Reymann AC, Guérin C, Martiel JL, De La Cruz EM, Blanchoin L. Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries. Current Biology 2011, 21: 862-868. PMID: 21530260, PMCID: PMC3100394, DOI: 10.1016/j.cub.2011.03.064.Peer-Reviewed Original ResearchDirect Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin
Shiroguchi K, Chin HF, Hannemann DE, Muneyuki E, De La Cruz EM, Kinosita K. Direct Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin. PLOS Biology 2011, 9: e1001031. PMID: 21532738, PMCID: PMC3075224, DOI: 10.1371/journal.pbio.1001031.Peer-Reviewed Original Research