Journal
SCIENCE
Volume 316, Issue 5821, Pages 120-123Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1136985
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Funding
- Medical Research Council [G0200542(63814), MC_U105184313, G0200542, U.1051.04.002(78842)] Funding Source: Medline
- Medical Research Council [G0200542, MC_U105184313] Funding Source: researchfish
- MRC [MC_U105184313, G0200542] Funding Source: UKRI
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Kinesin-1 is a two-headed molecular motor that walks along microtubules, with each step gated by adenosine triphosphate (ATP) binding. Existing models for the gating mechanism propose a role for the microtubule lattice. We show that unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate (ADP). With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-1 dimer binds two tubulin heterodimers. The data reveal an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of a steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head.
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