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Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function

Abstract

INOSITOL phospholipid turnover is enhanced during mitogenic stimulation of cells by growth factors1 and the breakdown of phosphatidylinositol 4,5-bisphosphate (PtdInsP2) may be important in triggering cell proliferation. PtdInsP2 also binds actin-binding proteins to regulate their activity2–7, but it is not yet understood how this control is achieved. The protein α-actinin from striated muscle contains large amounts of endogenous PtdInsP2, whereas that from smooth muscle has only a little but will bind exogenously added PtdInsP2. In vitro α-actinin binds to F-actin and will crosslink actin filaments, increasing the viscosity of F-actin solutions8,9. We report here that α-actinin from striated muscle is an endogenous PtdInsP2-bound protein and that the specific interaction between α-actinin and PtdInsP2 regulates the F-actin-gelating activity of α-actinin. Although the F-actin-gelating activity of α-actinin from smooth muscle is much reduced compared with that from striated muscle, exogenous PtdInsP2 can enhance the activity of smooth muscle α-actinin to the level seen in striated muscles. These results show that PtdInsP2 is present in striated muscle α-actinin and that it is necessary for α-actinin to realize its maximum gelating activity.

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References

  1. Rozengurt, E. Science 234, 161–166 (1986).

    Article  ADS  CAS  Google Scholar 

  2. Lassing, I. & Lindberg, U. Nature 314, 472–474 (1985).

    Article  ADS  CAS  Google Scholar 

  3. Janmey, P. A. & Stossel, T. P. Nature 325, 362–364 (1987).

    Article  ADS  CAS  Google Scholar 

  4. Janmey, P. A., Iida, K., Yin, H. L. & Stossel, T. P. J. biol. Chem. 262, 12228–12236 (1987).

    CAS  PubMed  Google Scholar 

  5. Yu, F., Johnston, P. A., Sudhof, T. C. & Yin, H. L. Science 250, 1413–1415 (1990).

    Article  ADS  CAS  Google Scholar 

  6. Heiss, S. H. & Cooper, J. A. Biochemistry 30, 8753–8758 (1991).

    Article  CAS  Google Scholar 

  7. Anderson, R. A. & Marchesi, V. T. Nature 318, 295–298 (1985).

    Article  ADS  CAS  Google Scholar 

  8. Ebashi, S., Ebashi, F. & Maruyama, K. Nature 203, 645–646 (1964).

    Article  ADS  CAS  Google Scholar 

  9. Maruyama, K. & Ebashi, S. J. Biochem. 58, 7–12 (1965).

    Article  Google Scholar 

  10. Matuoka, K., Fukami, K., Nakanishi, O., Kawai, S. & Takenawa, T. Science 239, 640–643 (1988).

    Article  ADS  CAS  Google Scholar 

  11. Masaki, T., Endo, M. & Ebashi, S. J. Biochem. 62, 630–632 (1967).

    Article  CAS  Google Scholar 

  12. Pollard, T. D. & Cooper, J. A. Meth. Enzym. 85, 211–233 (1982).

    Article  CAS  Google Scholar 

  13. Bennett, J. P., Zaner, K. S. & Stossel, T. P. Biochemistry 23, 5081–5086 (1984).

    Article  CAS  Google Scholar 

  14. Landon, F., Gache, Y., Touitou, H. & Olomucki, A. Eur. J. Biochem. 153, 231–237 (1985).

    Article  CAS  Google Scholar 

  15. Furuhashi, K., Inagaki, M., Hatano, S., Fukami, K. & Takenawa, T. Biochem. biophys. Res. Commun. 184, 121–1265 (1992).

    Article  Google Scholar 

  16. Meyer, R. K., Schindler, H. & Burger, M. M. Proc. natn. Acad. Sci. U.S.A. 79, 4280–4284 (1982).

    Article  ADS  CAS  Google Scholar 

  17. Burn, P., Rotman, A., Meyer, R. K. & Burger, M. M. Nature 314, 469–472 (1985).

    Article  ADS  CAS  Google Scholar 

  18. Endo, T. & Masaki, T. J. Biochem. 92, 1457–1468 (1982).

    Article  CAS  Google Scholar 

  19. Kobayashi, R., Itoh, H. & Tashima, Y. Eur. J. Biochem. 143, 125–131 (1984).

    Article  CAS  Google Scholar 

  20. Endo, T. & Masaki, T. Biochem. biophys. Res. Commun. 107, 1467–1474 (1982).

    Article  CAS  Google Scholar 

  21. Laemmli, U. K. Nature 227, 680–685 (1970).

    Article  ADS  CAS  Google Scholar 

  22. Khyse-Anderson, J. J. biochem. biophys. Meth. 10, 203–209 (1984).

    Article  Google Scholar 

  23. Feramisco, J. R. & Burridge, K. J. biol. Chem. 255, 1194–1199 (1980).

    CAS  Google Scholar 

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Fukami, K., Furuhashi, K., Inagaki, M. et al. Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function. Nature 359, 150–152 (1992). https://doi.org/10.1038/359150a0

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