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 functionFilamentsSubunitResiduesPublisher 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 mechanismArp2OrganellesNoncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin
Singh S, Siegler N, Pandey H, Yanir N, Popov M, Goldstein-Levitin A, Sadan M, Debs G, Zarivach R, Frank G, Kass I, Sindelar C, Zalk R, Gheber L. Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin. Science Advances 2024, 10: eadi1367. PMID: 38324691, PMCID: PMC10849588, DOI: 10.1126/sciadv.adi1367.Peer-Reviewed Original ResearchConceptsBidirectional motilityKinesin-5Plus-end-directed motilityKinesin-5 motorsCryo-EMC-terminal tailCryo-EM mapsPlus-end-directed kinesinCryo-electron microscopyDeletion mutantsNoncanonical interactionsIntracellular functionsCin8Cryo-electronMotor domainMotilityNonmotor domainsMutantsB-tubulinSingle-moleculeCell viabilityIn vivoIn vitroIn vitro experimentsLocal defects
2023
Twist 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
2021
An asymmetric structure of the filament is key to inducing flagellar curvature and enabling motility in the Leptospira spirochete
San Martin F, Gibson K, Trajtenberg F, Brady M, Wunder E, Picardeau M, Mechaly A, Ko A, Sindelar C, Buschiazzo A. An asymmetric structure of the filament is key to inducing flagellar curvature and enabling motility in the Leptospira spirochete. Acta Crystallographica Section A: Foundations And Advances 2021, 77: c291-c291. DOI: 10.1107/s0108767321093910.Peer-Reviewed Original Research
2020
New Techniques to Address Asymmetry in 3D Structure Analysis of Helical Biofilaments Imaged by Cryo-EM
Sindelar C, Debs G, Huehn A. New Techniques to Address Asymmetry in 3D Structure Analysis of Helical Biofilaments Imaged by Cryo-EM. Microscopy And Microanalysis 2020, 26: 1612-1612. DOI: 10.1017/s1431927620018711.Peer-Reviewed Original ResearchDynamic and asymmetric fluctuations in the microtubule wall captured by high-resolution cryoelectron microscopy
Debs GE, Cha M, Liu X, Huehn AR, Sindelar CV. Dynamic and asymmetric fluctuations in the microtubule wall captured by high-resolution cryoelectron microscopy. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 16976-16984. PMID: 32636254, PMCID: PMC7382274, DOI: 10.1073/pnas.2001546117.Peer-Reviewed Original ResearchAn asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete
Gibson KH, Trajtenberg F, Wunder EA, Brady MR, San Martin F, Mechaly A, Shang Z, Liu J, Picardeau M, Ko A, Buschiazzo A, Sindelar CV. An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete. ELife 2020, 9: e53672. PMID: 32157997, PMCID: PMC7065911, DOI: 10.7554/elife.53672.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyKey functional attributesNative flagellar filamentsHigh-resolution cryo-electron tomographyPeriplasmic spaceSheath proteinStructural basisFlagellar filamentsLeptospira spirochetesSpirochete bacteriaEntire cellFunctional attributesX-ray crystallographyImportant pathogenSupercoilingMotilityBacteriaFilamentsCell bodiesFlagellaSpirochetesProteinFlagellinDistinctive meansEndoflagellaIn Vitro Configuration of Munc13-1 Bridging of Phospholipid Bilayers at Resting Conditions
Grushin K, Sundaram R, Gibson K, Krishnakumar S, Sindelar C, Rothman J. In Vitro Configuration of Munc13-1 Bridging of Phospholipid Bilayers at Resting Conditions. Biophysical Journal 2020, 118: 400a. DOI: 10.1016/j.bpj.2019.11.2272.Peer-Reviewed Original ResearchStructures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments
Huehn AR, Bibeau JP, Schramm AC, Cao W, De La Cruz EM, Sindelar CV. Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 1478-1484. PMID: 31900364, PMCID: PMC6983403, DOI: 10.1073/pnas.1915987117.Peer-Reviewed Original ResearchConceptsFilament severingActin filamentsSevering activityCofilin/ADF familyActin conformational changesActin filament severingFilament-severing activityCryo-electron microscopy dataSevers actin filamentsWeak severing activityUnique binding modeCofilin clustersActin structuresCofilin bindingCofilin-decorated segmentsCofilinMolecular understandingBarbed endsConformational changesCooperative bindingBinding cooperativityFilament endsPositive cooperativityBinding modesSevering
2019
Severed Actin and Microtubules with Motors Walking All Over Them: Cryo-EM Studies of Seriously Perturbed Helical Assemblies
Debs G, Huehn A, Cha M, Liu X, Elam W, Cao W, De La Cruz E, Sindelar C. Severed Actin and Microtubules with Motors Walking All Over Them: Cryo-EM Studies of Seriously Perturbed Helical Assemblies. Microscopy And Microanalysis 2019, 25: 1362-1363. DOI: 10.1017/s1431927619007542.Peer-Reviewed Original ResearchStructural basis for the clamping and Ca2+ activation of SNARE-mediated fusion by synaptotagmin
Grushin K, Wang J, Coleman J, Rothman JE, Sindelar CV, Krishnakumar SS. Structural basis for the clamping and Ca2+ activation of SNARE-mediated fusion by synaptotagmin. Nature Communications 2019, 10: 2413. PMID: 31160571, PMCID: PMC6546687, DOI: 10.1038/s41467-019-10391-x.Peer-Reviewed Original ResearchConceptsCryo-electron microscopy structureActivation of SNAREsDependent membrane interactionsAnionic lipid headgroupsFusion clampActivator functionSNARE bundleSNARE proteinsMicroscopy structureC2B domainStructural basisSynaptotagmin-1SNAREpinsAliphatic loopsMembrane interactionsComplete assemblyLipid headgroupsLipid membranesNeurotransmitter releaseMembraneKey determinantSynaptotagminSyt1Calcium influxPartial insertion
2018
Structural basis of the filamin A actin-binding domain interaction with F-actin
Iwamoto DV, Huehn A, Simon B, Huet-Calderwood C, Baldassarre M, Sindelar CV, Calderwood DA. Structural basis of the filamin A actin-binding domain interaction with F-actin. Nature Structural & Molecular Biology 2018, 25: 918-927. PMID: 30224736, PMCID: PMC6173970, DOI: 10.1038/s41594-018-0128-3.Peer-Reviewed Original ResearchConceptsActin-binding domainCalponin homology domainHomology domainF-actinActin cross-linking proteinFunction mutationsTandem calponin homology domainsDisease-associated mutantsCryo-electron microscopyHigh-resolution structuresNumerous genetic diseasesSequence conservationHigher-order structureLinking proteinStructural basisDomain interactionsCell shapeActin filamentsMolecular understandingN-terminalFunctional studiesGenetic diseasesMissense mutationsMutationsAtomic resolutionThe actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments
Huehn A, Cao W, Elam WA, Liu X, De La Cruz EM, Sindelar CV. The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. Journal Of Biological Chemistry 2018, 293: 5377-5383. PMID: 29463680, PMCID: PMC5900768, DOI: 10.1074/jbc.ac118.001843.Peer-Reviewed Original ResearchConceptsCofilin-decorated segmentsConformational changesCofilin/ADF proteinsActin-remodeling proteinsBind actin filamentsActin filament interactionsCofilin-induced changesEffects of cofilinCooperative conformational changesProtein occupancyADF proteinsCellular processesCell divisionStructure-based methodsCryo-EMActin segmentsIntracellular transportActin filamentsFilament twistCooperative bindingCofilinTwist changesActinFluorophore labelingSubunitsStructural Characterization of the ATP-waiting and Post-hydrolysis States of Dimeric Kinesin-1 using Cryo-EM
Keun H, Liu X, Debs G, Liu D, Sindelar C. Structural Characterization of the ATP-waiting and Post-hydrolysis States of Dimeric Kinesin-1 using Cryo-EM. Biophysical Journal 2018, 114: 510a. DOI: 10.1016/j.bpj.2017.11.2788.Peer-Reviewed Original ResearchAccounting for Microtubule Distortions in Cryo-EM Structures using Patch Refinements
Debs G, Liu X, Keun H, Sindelar C. Accounting for Microtubule Distortions in Cryo-EM Structures using Patch Refinements. Biophysical Journal 2018, 114: 164a. DOI: 10.1016/j.bpj.2017.11.916.Peer-Reviewed Original ResearchStructural Insight into the Interaction of Synaptotagmin-1 and Snare Complex on Lipid Bilayer by Cryo-Electron Microscopy
Grushin K, Wang J, Coleman J, Rothman J, Sindelar C, Krishnakumar S. Structural Insight into the Interaction of Synaptotagmin-1 and Snare Complex on Lipid Bilayer by Cryo-Electron Microscopy. Biophysical Journal 2018, 114: 282a. DOI: 10.1016/j.bpj.2017.11.1622.Peer-Reviewed Original ResearchNovel Architecture and Composition of a Bacterial Flagellum in the Spirochete Leptospira biflexa
Gibson K, Wunder E, Liu J, Trajtenberg F, Buschiazzo A, Ko A, Sindelar C. Novel Architecture and Composition of a Bacterial Flagellum in the Spirochete Leptospira biflexa. Biophysical Journal 2018, 114: 371a. DOI: 10.1016/j.bpj.2017.11.2056.Peer-Reviewed Original ResearchCofilin Induces a Local Change in the Twist of Actin Filaments
Huehn A, Cao W, Elam W, De La Cruz E, Sindelar C. Cofilin Induces a Local Change in the Twist of Actin Filaments. Biophysical Journal 2018, 114: 145a. DOI: 10.1016/j.bpj.2017.11.812.Peer-Reviewed Original Research