Ca2+-calmodulin-dependent regulation of F-actin-myelin basic protein interaction

Abstract

Myelin basic proteins (MBP) interacts with F-actin resulting in the precipitation of a complex of both proteins. Electron microscope observations of this complex reveal the presence of ordered bundles of F-actin filaments similar to those obtained from F-actin and troponin I. In addition to the bundles, there also appear short fragments of F-actin filaments. In the presence of Ca2+ calmodulin causes a release of MBP from its complex with F-actin, accompanied by dissociation of F-actin bundles into separate filaments. Parallel to the binding of MBP to F-actin the ATPase activity of actomyosin is progressively reduced. This inhibition is reversed by calmodulin but only in the presence of Ca2+. Studies of the binding of S-1 to F-actin and to the F-actin-MBP complex indicate that the interaction sites for MBP and S-1 on the actin molecule are different.