An ATP Gate Controls Tubulin Binding by the Tethered Head of Kinesin-1

Overview

Journal Science

Specialty Science

Date 2007 Apr 7

PMID 17412962

Citations 57

Authors

Maria C Alonso

Douglas R Drummond

Susan Kain

Julia Hoeng

Linda Amos

Robert A Cross

Affiliations

Soon will be listed here.

Abstract

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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