An ATP gate controls tubulin binding by the tethered head of kinesin-1

Maria C. Alonso, Douglas R. Drummond, Susan Kain, Julia Hoeng, Linda Amos, Robert A. Cross

Research output: Contribution to journalArticlepeer-review

96 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)120-123
Number of pages4
Issue number5821
Publication statusPublished - Apr 6 2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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