Journal of Biological Chemistry
Open access logo
Advanced SearchSave search
Journal Article| Volume 265, ISSUE 15, P8382-8386, May 25, 1990

Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides.

Open AccessDOI:https://doi.org/10.1016/S0021-9258(19)38897-0
Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides.
Previous ArticlePrimary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells.
Next ArticleHistidine 235 of human sex hormone-binding globulin is the covalent site of attachment of the nucleophilic steroid derivative, 17 beta-bromoacetoxydihydrotestosterone.
      This paper is only available as a PDF. To read, Please Download here.
      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.

      REFERENCES

        • Nishida E.
        • Maekawa S.
        • Sakai H.
        Biochemistry. 1984; 23: 5307-5313
        • Nishida E.
        Biochemistry. 1985; 24: 1160-1164
        • Muneyuki E.
        • Nishida E.
        • Sutoh K.
        • Sakai H.
        J. Biochem. (Tokyo). 1985; 97: 563-568
        • Nishida E.
        • Iida K.
        • Yonezawa N.
        • Koyasu S.
        • Yahara I.
        • Sakai H.
        Proc. Natl. Acad. Sci. U. S. A. 1987; 84: 5262-5266
        • Yonezawa N.
        • Nishida E.
        • Koyasu S.
        • Maekawa S.
        • Ohta Y.
        • Yahara I.
        • Sakai H.
        Cell Struct. Funct. 1987; 12: 443-452
        • Yonezawa N.
        • Nishida E.
        • Sakai H.
        J. Biol. Chem. 1985; 260: 14410-14412
        • Matsuzaki F.
        • Matsumoto S.
        • Yahara I.
        • Yonezawa N.
        • Nishida E.
        • Sakai H.
        J. Biol. Chem. 1988; 263: 11564-11568
        • Nishida E.
        • Maekawa S.
        • Muneyuki E.
        • Sakai H.
        J. Biochem. (Tokyo). 1984; 95: 387-398
        • Nishida E.
        • Muneyuki E.
        • Maekawa S.
        • Ohta Y.
        • Sakai H.
        Biochemistry. 1985; 24: 6624-6630
        • Maekawa S.
        • Nishida E.
        • Ohta Y.
        • Sakai H.
        J. Biochem. (Tokyo). 1984; 95: 377-385
        • Bamburg J.R.
        • Harris H.E.
        • Weeds A.G.
        FEBS Lett. 1980; 121: 178-182
        • Giuliano K.A.
        • Khatib F.A.
        • Hayden S.M.
        • Daoud E.W.R.
        • Adams M.E.
        • Amorese D.A.
        • Bernstein B.W.
        • Bamburg J.R.
        Biochemistry. 1988; 27: 8931-8938
        • Mabuchi I.
        J. Cell Biol. 1983; 97: 1612-1621
        • Cooper J.A.
        • Blum J.D.
        • Williams Jr., R.C.
        • Pollard T.D.
        J. Biol. Chem. 1986; 261: 477-485
        • Moriyama K.
        • Nishida E.
        • Yonezawa N.
        • Sakai H.
        • Matsumoto S.
        • Iida K.
        • Yahara L
        J. Biol. Chem. 1990; 265: 5768-5773
        • Lassing I.
        • Lindberg U.
        Nature. 1985; 314: 472-474
        • Janmey P.A.
        • Stossel T.P.
        Nature. 1987; 325: 362-364
        • Janmey P.A.
        • lida K.
        • Yin H.L.
        • Stossel T.P.
        J. Biol. Chem. 1987; 262: 12228-12236
        • Janmey P.A.
        • Matsudaira P.T.
        J. Biol. Chem. 1988; 263: 16738-16743
        • Hartwig J.H.
        • Chambers K.A.
        • Stossel T.P.
        J. Cell. Biol. 1989; 108: 467-479
        • Spudich J.A.
        • Watt S.
        J. Biol. Chem. 1971; 246: 4866-4871
        • Yonezawa N.
        • Nishida E.
        • Maekawa S.
        • Sakai H.
        Biochem. J. 1988; 251: 121-127
        • Laemmli U.K.
        Nature. 1970; 227: 680-685
        • Blikstad I.
        • Markey F.
        • Carlsson L.
        • Person T.
        • Lindberg U.
        Cell. 1978; 15: 935-943
        • Brenner S.L.
        • Korn E.D.
        J. Biol. Chem. 1983; 258: 5013-5020
        • Sugiura Y.
        Biochim. Biophys. Acta. 1981; 641: 148-159
        • Lazarides E.
        • Lindberg U.
        Proc. Natl. Acad. Sci. U. & A. 1974; 71: 4742-4746
        • Hitchcock S.E.
        • Carlsson L.
        • Lindberg U.
        Cell. 1976; 7: 531-542
        • Mannherz H.G.
        • Goody R.S.
        • Konrad M.
        • Nowak E.
        Eur. J. Biochem. 1980; 104: 367-379
        • Sutoh K.
        • Yin H.L.
        Biochemistry. 1989; 28: 5269-5275
        • Sutoh K.
        Biochemistry. 1984; 23: 1942-1946
        • Yin H.L.
        • lida K.
        • Janmey P.A.
        J. Cell Biol. 1988; 106: 805-812
        • Kwiatkowski D.J.
        • Janmey P.A.
        • Yin H.L.
        J. Cell Biol. 1989; 108: 1717-1726
        • Burn P.
        • Rotman A.
        • Meyer R.K.
        • Burger M.M.
        Nature. 1985; 314: 469-472

      Article Info

      Identification

      DOI: https://doi.org/10.1016/S0021-9258(19)38897-0

      Copyright

      © 1990 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

      User License

      Creative Commons Attribution – NonCommercial – NoDerivs (CC BY-NC-ND 4.0) |
      How you can reuse Information Icon
      Creative Commons Attribution – NonCommercial – NoDerivs (CC BY-NC-ND 4.0)

      Permitted

      For non-commercial purposes:

      • Read, print & download
      • Redistribute or republish the final article
      • Text & data mine
      • Translate the article (private use only, not for distribution)
      • Reuse portions or extracts from the article in other works

      Not Permitted

      • Sell or re-use for commercial purposes
      • Distribute translations or adaptations of the article

      Elsevier's open access license policy

      ScienceDirect

      Access this article on ScienceDirect

      ASBMB  ASBMB  ASBMB  ASBMB

      ISSN 0021-9258

      We use cookies to help provide and enhance our service and tailor content and ads. By continuing you agree to the Use of Cookies.
      Copyright © 2021 American Society for Biochemistry and Molecular Biology. Published by Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology. All rights reserved.


      RELX