Wenxiang Cao, PhD
Research ScientistCards
About
Research
Publications
2024
High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations
Xu X, Cao W, Swift M, Pandit N, Huehn A, Sindelar C, De La Cruz E, Hanein D, Volkmann N. High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations. Communications Chemistry 2024, 7: 164. PMID: 39079963, PMCID: PMC11289367, DOI: 10.1038/s42004-024-01243-x.Peer-Reviewed Original ResearchActin filamentsVertebrate actinsActin structuresDNase I binding loopActin filament assemblyEukaryotic cell functionStructures of wild-typeNear-atomic resolution structuresPotential binding sitesActin subunitsFilament assemblyRegulatory proteinsDNase IA167ActinAdjacent subunitsRegulatory roleMolecular mechanismsVertebratesWild-typeGlutamic acidCell functionFilamentsSubunitResiduesQuantitative correlation of ENPP1 pathogenic variants with disease phenotype
Ansh A, Stabach P, Ciccone C, Cao W, De La Cruz E, Sabbagh Y, Carpenter T, Ferreira C, Braddock D. Quantitative correlation of ENPP1 pathogenic variants with disease phenotype. Bone 2024, 186: 117136. PMID: 38806089, PMCID: PMC11227391, DOI: 10.1016/j.bone.2024.117136.Peer-Reviewed Original ResearchEctonucleotide pyrophosphatase/phosphodiesterase 1Pathogenic variantsDisease phenotypeEnzyme velocityCompound heterozygotesEnzyme activityVariable enzyme activityAutosomal dominant phenotypeHigh-throughput assayAutosomal recessive formInnate immune responseENPP1 variantsDamaging variantsENPP1 deficiencyCole diseaseDominant phenotypeAutosomal dominant diseaseCatalytic velocityRecessive formEnzymePhenotypeWT levelsBio-active moleculesClinical phenotypeDominant diseasePublisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2354. PMID: 38491023, PMCID: PMC10943100, DOI: 10.1038/s41467-024-46804-9.Peer-Reviewed Original ResearchCryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2059. PMID: 38448439, PMCID: PMC10918085, DOI: 10.1038/s41467-024-46179-x.Peer-Reviewed Original ResearchConceptsArp2/3 complexActin filamentsCryo-EM structureMother filamentDaughter filamentArp2/3 complex nucleates branched actin filamentsActin filament branchingBranched actin filamentsDissociation of PiADP-PiFilament branchingOrganelle movementADP stateBranch junctionsArp3A-resolutionActinArp2/3ADP-BeFxFilamentsADPPhosphate releaseFilament mechanismArp2OrganellesDistinct functional constraints driving conservation of the cofilin N-terminal regulatory tail
Sexton J, Potchernikov T, Bibeau J, Casanova-Sepúlveda G, Cao W, Lou H, Boggon T, De La Cruz E, Turk B. Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail. Nature Communications 2024, 15: 1426. PMID: 38365893, PMCID: PMC10873347, DOI: 10.1038/s41467-024-45878-9.Peer-Reviewed Original ResearchConceptsN-terminal regionActin bindingSequence requirementsLIM kinaseAnalysis of individual variantsInactivates cofilinS. cerevisiaeRegulatory tailFamily proteinsActin depolymerizationPhosphorylation sitesKinase recognitionSequence variantsInhibitory phosphorylationCofilinN-terminusIndividual variantsFunctional constraintsActinDisordered sequencesPhosphorylationSequenceBiochemical analysisSequence constraintsKinase
2023
Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change
Sun Z, Yadav V, Amiri S, Cao W, De La Cruz E, Murrell M. Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change. European Journal Of Cell Biology 2023, 103: 151379. PMID: 38168598, DOI: 10.1016/j.ejcb.2023.151379.Peer-Reviewed Original ResearchCooperative ligand binding to a double-stranded Ising lattice—Application to cofilin binding to actin filaments
Cao W, Taylor E, De La Cruz E. Cooperative ligand binding to a double-stranded Ising lattice—Application to cofilin binding to actin filaments. PNAS Nexus 2023, 2: pgad331. PMID: 37885622, PMCID: PMC10599439, DOI: 10.1093/pnasnexus/pgad331.Peer-Reviewed Original ResearchExact solutionCluster sizeIsing latticeLattice systemsBest fit parametersTransfer matrix methodInfinite onesChemical physicsMatrix methodCooperative ligandFit parametersLigand binding interactionsLinear polymersAdditional experimental informationBinding interactionsIsingSolutionDouble-stranded modelAnalysis of varietyLigandsElectron microscopyPolymersExperimental informationExperimental observationsPhysicsFriction patterns guide actin network contraction
Colin A, Orhant-Prioux M, Guérin C, Savinov M, Cao W, Vianay B, Scarfone I, Roux A, De La Cruz E, Mogilner A, Théry M, Blanchoin L. Friction patterns guide actin network contraction. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2300416120. PMID: 37725653, PMCID: PMC10523593, DOI: 10.1073/pnas.2300416120.Peer-Reviewed Original ResearchConceptsFriction forceTwist response of actin filaments
Bibeau J, Pandit N, Gray S, Nejad N, Sindelar C, Cao W, De La Cruz E. Twist response of actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2208536120. PMID: 36656858, PMCID: PMC9942836, DOI: 10.1073/pnas.2208536120.Peer-Reviewed Original Research
2022
Flagella-like beating of actin bundles driven by self-organized myosin waves
Pochitaloff M, Miranda M, Richard M, Chaiyasitdhi A, Takagi Y, Cao W, De La Cruz E, Sellers J, Joanny J, Jülicher F, Blanchoin L, Martin P. Flagella-like beating of actin bundles driven by self-organized myosin waves. Nature Physics 2022, 18: 1240-1247. PMID: 37396880, PMCID: PMC10312380, DOI: 10.1038/s41567-022-01688-8.Peer-Reviewed Original Research