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The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by recruiting it to the microtubule.
journal contribution
posted on 2005-04-01, 00:00 authored by Heidi Browning, David HackneyDavid HackneyTea2 is a kinesin family member from Schizosaccharomyces pombe that is targeted to microtubule tips and cell ends in a process that depends on Mal3. Constructs of Tea2 containing the motor domain only or the motor domain plus the N-terminal extension are monomeric, whereas a construct including the first predicted coiled coil region is dimeric. These constructs have a low basal rate of ATP hydrolysis of
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2005-04-01Usage metrics
Keywords
Adenosine TriphosphatasesAdenosine TriphosphateBinding SitesDimerizationDose-Response RelationshipDrugElectrophoresisPolyacrylamide GelHydrolysisKineticsMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein StructureTertiaryProtein TransportSchizosaccharomycesSchizosaccharomyces pombe ProteinsTemperatureTime Factors