We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Myosin VI is an actin-based motor that moves backwards.
- Authors
Wells, A L; Lin, A W; Chen, L Q; Safer, D; Cain, S M; Hasson, T; Carragher, B O; Milligan, R A; Sweeney, H L
- Abstract
Myosins and kinesins are molecular motors that hydrolyse ATP to track along actin filaments and microtubules, respectively. Although the kinesin family includes motors that move towards either the plus or minus ends of microtubules, all characterized myosin motors move towards the barbed (+) end of actin filaments. Crystal structures of myosin II (refs 3-6) have shown that small movements within the myosin motor core are transmitted through the 'converter domain' to a 'lever arm' consisting of a light-chain-binding helix and associated light chains. The lever arm further amplifies the motions of the converter domain into large directed movements. Here we report that myosin VI, an unconventional myosin, moves towards the pointed (-) end of actin. We visualized the myosin VI construct bound to actin using cryo-electron microscopy and image analysis, and found that an ADP-mediated conformational change in the domain distal to the motor, a structure likely to be the effective lever arm, is in the opposite direction to that observed for other myosins. Thus, it appears that myosin VI achieves reverse-direction movement by rotating its lever arm in the opposite direction to conventional myosin lever arm movement.
- Publication
Nature, 1999, Vol 401, Issue 6752, p505
- ISSN
0028-0836
- Publication type
Journal Article
- DOI
10.1038/46835