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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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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DOI: https://doi.org/10.1038/359150a0
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