Kinesin's tail domain is an inhibitory regulator of the motor domain

David L. Coy, William O. Hancock, Michael Wagenbach, Jonathon Howard

Research output: Contribution to journalArticle

203 Scopus citations

Abstract

When not bound to cargo, the motor protein kinesin is in an inhibited state that has low microtubule-stimulated ATPase activity. Inhibition serves to minimize the dissipation of ATP and to prevent mislocalization of kinesin in the cell. Here we show that this inhibition is relieved when kinesin binds to an artificial cargo. Inhibition is mediated by kinesin's tail domain: deletion of the tail activates the ATPase without need of cargo binding, and inhibition is re-established by addition of exogenous tail peptide. Both ATPase and motility assays indicate that the tail does not prevent kinesin from binding to microtubules, but rather reduces the motor's stepping rate.

Original languageEnglish (US)
Pages (from-to)288-292
Number of pages5
JournalNature Cell Biology
Volume1
Issue number5
DOIs
StatePublished - Jan 1 1999

All Science Journal Classification (ASJC) codes

  • Cell Biology

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