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 Research
2011
Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing
McCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM. Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing. Biophysical Journal 2011, 101: 151-159. PMID: 21723825, PMCID: PMC3127193, DOI: 10.1016/j.bpj.2011.05.049.Peer-Reviewed Original Research