INOSITOL PHOSPHOLIPID - INDUCED SUPPRESSION OF F-ACTIN-GELATING ACTIVITY OF SMOOTH-MUSCLE FILAMIN

Filamin, a high molecular weight actin-binding protein, cross-links actin filaments and produces a gel composed of Factin. The effects of polyphosphoinositides on the gelating activity of smooth muscle filamin were examined by measuring the low shear viscosity of the F-actin solutions containing filamin incubated with phosphatidylinositol (PI), phosphatidylinositol 4-monophosphate (PIP), or phosphatidylinositol 4,5-bisphosphate (PIP2). Micelles of these inositol phospholipids bound to filamin inhibited the ability to form a gel of F-actin. The inhibiting activity of each phospholipid was in the following order, PIP2 > PIP > PI. The F-actin binding assay of filamin revealed that the inhibition of F-actin-gelation resulted in the loss of the F-actin-binding activity of filamin. Thus, polyphosphoinositides may play important roles in regulating the gelating activity of filamin. © 1992 Academic Press, Inc.