Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function - PubMed (original) (raw)
. 1992 Sep 10;359(6391):150-2.
doi: 10.1038/359150a0.
Affiliations
- PMID: 1326084
- DOI: 10.1038/359150a0
Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function
K Fukami et al. Nature. 1992.
Abstract
Inositol phospholipid turnover is enhanced during mitogenic stimulation of cells by growth factors 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 activity, but it is not yet understood how this control is achieved. The protein alpha-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 alpha-actinin binds to F-actin and will crosslink actin filaments, increasing the viscosity of F-actin solutions. We report here that alpha-actinin from striated muscle is an endogenous PtdInsP2-bound protein and that the specific interaction between alpha-actinin and PtdInsP2 regulates the F-actin-gelating activity of alpha-actinin. Although the F-actin-gelating activity of alpha-actinin from smooth muscle is much reduced compared with that from striated muscle, exogenous PtdInsP2 can enhance the activity of smooth muscle alpha-actinin to the level seen in striated muscles. These results show that PtdInsP2 is present in striated muscle alpha-actinin and that it is necessary for alpha-actinin to realize its maximum gelating activity.
Comment in
- Lipid-cytoskeleton interactions.
Niggli V. Niggli V. Nature. 1993 Jan 21;361(6409):214. doi: 10.1038/361214b0. Nature. 1993. PMID: 8380904 No abstract available.
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