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Decision letter: The kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding
Kinesin-5 motors organize mitotic spindles by sliding apart microtubules. They are homotetramers with dimeric motor and tail domains at both ends of a bipolar minifilament. Here, we describe a regulatory mechanism involving direct binding between tail and motor domains and its fundamental role in microtubule sliding. Kinesin-5 tails decrease microtubule-stimulated ATPhydrolysis by specifically engaging motor domains in the nucleotide-free or ADP states. Cryo-EM reveals that tail bindingdoi:10.7554/elife.51131.sa1 fatcat:6xf7wr3ukzdkpht7dot6sk3keq