Reconsidering the Lever-Arm Theory of Myosin Action

Abstract

It is widely believed that myosin generates force by swinging its light-chain binding domain (lever arm) on the motor domain, which is affixed firmly onto actin via stereospecific hydrophobic interactions. However, recent results suggest that the events taking place at the actin-myosin interface are more dynamic than previously considered. This brief review discusses some of the results which suggest such dynamic nature of actin-myosin interface in relation to the conventional understanding.