Journal
MOLECULAR CELL
Volume 35, Issue 3, Pages 305-315Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2009.07.010
Keywords
-
Categories
Funding
- National Institutes of Health (NIH)
- Centre National de la Recherche Scientifique (CNRS)
- ANR [BLAN07-3193368]
- ACI BCMS
- American Heart Association
Ask authors/readers for more resources
Myosin VI challenges the prevailing theory of how myosin motors move on actin: the lever arm hypothesis. While the reverse directionality and large power-stroke of myosin VI can be attributed to unusual properties of a subdomain of the motor (converter with a unique insert), these adaptations cannot account for the large step size on actin. Either the lever arm hypothesis needs modification, or myosin VI has some unique form of extension of its lever arm. We determined the structure of the region immediately distal to the lever arm of the motor and show that it is a three-helix bundle. Based on C-terminal truncations that display the normal range of step sizes on actin, CID, fluorescence studies, and a partial deletion of the bundle, we demonstrate that this bundle unfolds upon dimerization of two myosin VI monomers. This unconventional mechanism generates an extension of the lever arm of myosin VI.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available