2020
Cutting, Amplifying, and Aligning Microtubules with Severing Enzymes
Kuo YW, Howard J. Cutting, Amplifying, and Aligning Microtubules with Severing Enzymes. Trends In Cell Biology 2020, 31: 50-61. PMID: 33183955, PMCID: PMC7749064, DOI: 10.1016/j.tcb.2020.10.004.Peer-Reviewed Original ResearchConceptsAAA ATPasesTissue morphogenesisCellular processesMicrotubule cytoskeletonCell divisionGrowth promotionBiophysical advancesSevering enzymesMicrotubule networkMolecular mechanismsStrong promoterMicrotubule growthNeuronal developmentShort filamentsMicrotubulesSpastinEnzymeSeveringFidgetinKataninCytoskeletonMorphogenesisPromoterProteinRecent work
2019
Spastin is a dual-function enzyme that severs microtubules and promotes their regrowth to increase the number and mass of microtubules
Kuo YW, Trottier O, Mahamdeh M, Howard J. Spastin is a dual-function enzyme that severs microtubules and promotes their regrowth to increase the number and mass of microtubules. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 5533-5541. PMID: 30837315, PMCID: PMC6431158, DOI: 10.1073/pnas.1818824116.Peer-Reviewed Original ResearchConceptsDual-function enzymeMicrotubule dynamicsMass of microtubulesMicrotubule cytoskeletonDynamic cellular processesCellular processesMicrotubule regrowthNeuronal morphogenesisSevering activityVivo phenotypeMicrotubule assaysMicrotubulesNumber of microtubulesSpastinMicrotubule fragmentsRescue frequencyShort fragmentsCytoskeletonMicrotubule massObserved exponential increaseEnzymeRemodelersFidgetinKataninCiliogenesis
2008
XMAP215 Is a Processive Microtubule Polymerase
Brouhard GJ, Stear JH, Noetzel TL, Al-Bassam J, Kinoshita K, Harrison SC, Howard J, Hyman AA. XMAP215 Is a Processive Microtubule Polymerase. Cell 2008, 132: 79-88. PMID: 18191222, PMCID: PMC2311386, DOI: 10.1016/j.cell.2007.11.043.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBiological AssayCatalytic DomainCell DifferentiationCell EnlargementCell LineCytoskeletonDiffusionDimerizationFetal ProteinsForminsGreen Fluorescent ProteinsMicrofilament ProteinsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesNuclear ProteinsPolymersProtein BindingProtein Structure, TertiaryProtein TransportSpodopteraSus scrofaTubulinXenopus laevisXenopus ProteinsConceptsFamily of proteinsSingle-molecule assaysActin polymerasesMicrotubule cytoskeletonProcessive polymeraseTubulin subunit additionDynamic microtubulesMicrotubule polymeraseMicrotubule growthCytoskeletal polymersXMAP215Plus endsMicrotubule latticePolymeraseSubunit additionCell proliferationFree tubulinTubulin dimersMicrotubulesCommon mechanismFast growthTip trackingGrowthCytoskeletonRapid assembly
2006
Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner
Varga V, Helenius J, Tanaka K, Hyman AA, Tanaka TU, Howard J. Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner. Nature Cell Biology 2006, 8: 957-962. PMID: 16906145, DOI: 10.1038/ncb1462.Peer-Reviewed Original ResearchConceptsKinesin-8 proteinsLength-dependent depolymerizationYeast kinesin-8Length-dependent mannerMetazoan cellsMicrotubule cytoskeletonMitotic spindleDisassemble microtubulesSpindle lengthKinesin-8Kinesin-13Kip3pPlus endsMicrotubulesConstituent microtubulesLong microtubulesNew mechanismCytoskeletonFungiKinesinProteinSpindleCells