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J. Biol. Chem., Vol. 265, Issue 15, 8382-8386, May, 1990
N Yonezawa, E Nishida, K Iida, I Yahara and H Sakai
Cofilin is a widely distributed actin-modulating protein that has the
ability to bind along the side of F-actin and to depolymerize F-actin in a
pH-dependent manner. We found that phosphatidylinositol (PI),
phosphatidylinositol 4-monophosphate (PIP), and phosphatidylinositol
4,5-bisphosphate (PIP2) inhibited both actions of cofilin in a dose-
dependent manner, while inositol 1,4,5-triphosphate (IP3), 1-oleoyl-2-
acetylglycerol (OAG), phosphatidylserine (PS), or phosphatidylcholine (PC)
had little or no effect on them. Gel filtration analyses showed that PIP2
bound to cofilin and thereby inhibited the binding of cofilin to G-actin.
Destrin is a mammalian, pH-independent actin-depolymerizing protein. The
actin-depolymerizing activity of destrin was also inhibited by PI, PIP, and
PIP2, but not by IP3, OAG, PS, or PC. In addition, we found further that an
actin-depolymerizing activity of bovine pancreas deoxyribonuclease I, a
G-actin-sequestering protein, was inhibited by PIP and PIP2, but not by PI,
IP3, OAG, PS, or PC. These results together with previous findings
(Lassing, I., and Lindberg, U. (1985) Nature 314, 472-474; Janmey, P. A.,
and Stossel, T. P. (1987) Nature 325, 362-364) suggest that the sensitivity
to polyphosphoinositides may be a common feature in vitro among actin-
binding proteins that can bind to G-actin and regulate the state of actin
polymerization.
Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
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