2025
High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory
Chavali S, Carman P, Shuman H, Ostap E, Sindelar C. High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2415457122. PMID: 40014570, PMCID: PMC11892617, DOI: 10.1073/pnas.2415457122.Peer-Reviewed Original ResearchConceptsN-terminal extensionATP bindingRegulating ATP bindingADP releaseClass I myosinsLever arm swingStructure of myosinCryo-EM structureHigh-resolution structuresMembrane-bound vesiclesActin interfaceMyosin superfamilyMyosin familyActin filamentsAbsence of ADPMembrane remodelingNucleotide pocketMotile behaviorMyo1cPlasma membraneBiological functionsActinCryo-EM dataMotor domainMyosin
2024
Noncanonical 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
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