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
2014
Site-specific cation release drives actin filament severing by vertebrate cofilin
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 17821-17826. PMID: 25468977, PMCID: PMC4273407, DOI: 10.1073/pnas.1413397111.Peer-Reviewed Original ResearchConceptsFilament severingActin filamentsActin filament severingKey regulatory functionsConcentration of endsActin filament fragmentationEukaryotic cellsCation-binding sitesProtein cofilinDeletion mutantsS. cerevisiaeSubunit exchangeFilament turnoverActin polymerizationEssential functionsSite-specific interactionsCofilinMolecular mechanismsAssembly dynamicsRegulatory functionsActin moleculesFilament fragmentationFilament structureSustained motilitySevering