Abstract
Many actin-binding proteins have been purified from different cell types, and a number of them share certain features: they are affected by calcium in their interaction with actin and have similar subunit molecular weights (∼100,000) on SDS-poly-acrylamide gels. These proteins have been given various names, including gelsolin1–3, villin4,5, actinogelin6,7, Dictyostelium 95K protein8,9, platelet 95K protein10 and Acanthamoeba 85K protein11. The actin-binding protein α-actinin has received little attention in this analysis, even though it has a subunit molecular weight in this range (∼100,000) and has been shown immunologically to exist in non-muscle cells12,13. Here we report that α-actinin purified from HeLa cells is inhibited from cross-linking actin filaments by micromolar free calcium. In many properties it closely resembles actinogelin, Dictyostelium 95K protein and Acanthamoeba 85K protein, but it appears distinct from proteins such as gelsolin and villin which, in the presence of calcium, fragment actin filaments into short oligomers3,5. We conclude that in this molecular weight range there are at least two classes of non-muscle actin-binding protein: one corresponding to non-muscle α-actinins and the other to proteins such as gelsolin and villin.
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References
Yin, H. L. & Stossel, T. P. Nature 281, 583–586 (1979).
Yin, H. L. & Stossel, T. P. J. biol. Chem. 255, 9490–9493 (1980).
Yin, H. L., Zaner, K. S. & Stossel, T. P. J. biol. Chem. 255, 9494–9500 (1980).
Bretscher, A. & Weber, K. Proc. natn. Acad. Sci. U.S.A. 75, 2321–2325 (1975).
Bretscher, A. & Weber, K. Cell 20, 839–847 (1980).
Mimura, N. & Asano, A. Nature 272, 273–276 (1978).
Mimura, N. & Asano, A. Nature 282, 44–48 (1979).
Hellewell, S. B. & Taylor, D. L. J. Cell Biol. 83, 633–648 (1979).
Condeelis, J. in International Cell Biology (ed. Sweiger, H. G.) 306–320 (Springer, Berlin, 1981).
Wang, L.-L. & Bryan, J. J. Cell Biol. 87, 224a (1980).
Pollard, T. D. J. biol. Chem. 256, 7666–7670 (1981).
Lazarides, E. & Burridge, K. Cell 6, 289–298 (1975).
Schollmeyer, J. V., Furcht, L. T., Goll, D. E., Robson, R. M. & Stromer, M. M. in Cell Motility (eds Goldman, R., Pollard, T. D. & Rosenbaum, J.) 361–388 (Cold Spring Harbor Laboratory, New York, 1976).
Feramisco, J. R. & Burridge, K. J. biol. Chem. 255, 1194–1201 (1980).
Rosenberg, S., Stracher, A. & Burridge, K. J. biol. Chem. (in the press).
Hasegawa, T., Takahashi, S., Hayashi, H. & Hatano, S. Biochemistry 19, 2677–2683 (1980).
Hinssen, H. in Cell Motility: Molecules and Organization (eds Hatano, S., Ishikawa, H. & Sato, H.) 59–85 (University of Tokyo Press, 1979).
Burridge, K. & McCullough, L. J. supramolec. Struct. 13, 53–65 (1980).
Burridge, K. Meth. Enzym. 50, 54–63 (1978).
Laemmli, U. K. Nature 227, 680–685 (1970).
MacLean-Fletcher, S. D. & Pollard, T. D. J. Cell Biol. 85, 414–428 (1980).
Amos, W. B., Routledge, L. M., Weis-Fogh, T. & Yew, F. F. Soc. exp. Biol. 30, 273–301 (1976).
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Burridge, K., Feramisco, J. Non-muscle α-actinins are calcium-sensitive actin-binding proteins. Nature 294, 565–567 (1981). https://doi.org/10.1038/294565a0
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DOI: https://doi.org/10.1038/294565a0
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