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Diacylglycerol in large α-actinin/actin complexes and in the cytoskeleton of activated platelets

Nature volume 314, pages 469–472 (1985)Cite this article

Abstract

The interaction of the cytoskeleton with plasma membranes may be mediated by vinculin1–4, α-actinin5,6 and other proteins7–11; α-actinin can interact specifically with model membranes only if they contain diacylglycerol and palmitic acid12. On stimulation of platelets by thrombin, which leads to a reorganization of the cytoskeleton13–15, diacylglycerol is produced rapidly16, simultaneously with the disappearance of phosphatidylinositol16–19. One important function of the diacylglycerol produced in platelets may be the activation of the Ca2+- and phospholipid-dependent protein kinase C20–22 We show here that, in the presence of diacylglycerol and palmitic acid, a supramolecular complex between α-actinin and actin is formed in vitro. In the electron microscope, this complex displays substructures similar to those of microfilament bundles in vivo. Furthermore, such α-actinin/lipid complexes can also be formed in situ during the stimulation of blood platelet aggregation. Thus, α-actinin may be one of the proteins directly involved in structures connecting the cytoskeleton to cell membranes.

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Authors and Affiliations

  1. Department of Biochemistry, Biocenter of the University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland

    Paul Burn, A. Rotman, R. K. Meyer & Max M. Burger

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  1. Paul Burn
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  2. A. Rotman
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  3. R. K. Meyer
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Burn, P., Rotman, A., Meyer, R. et al. Diacylglycerol in large α-actinin/actin complexes and in the cytoskeleton of activated platelets. Nature 314, 469–472 (1985). https://doi.org/10.1038/314469a0

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