Abstract
One of the major filamentous systems of non-muscle cells is based on actin, a highly conserved protein of 42kD. The polymerization equilibrium between globular (G-) and filamentous (F-) actin determines the viscosity of the cytoplasm and is regulated by cytoplasmic salt conditions and by actin-binding proteins (for review see Stossel et al., 1985, Pollard and Cooper, 1986). Several of these actin-binding proteins are activated or inhibited by micromolar Ca2+-concentrations either through direct binding to Ca2+ or indirectly through modulators such as calmodulin.
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References
Ampe, C., and Vandekerckhove, J., 1987, The F-actin capping proteins of Physarum polycephalum : Cap42(a) is very similar, if not identical, To fragmin and structurally and functionally very homologous to gelsolin. Cap42(b) is Physarum actin, EMBO J., 6:4149–4157.
André, E., Lottspeich, F., Schleicher, M., and Noegel, A., 1988, Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains, J. Biol. Chem., 263:722–727.
Arimura, C., Suzuki, T., Yanagisawa, M., Imamura, M., Hamada, Y., and Masaki, T., 1988, Primary struc-ture of skeletal muscle and fibroblast actinins deduced from cDNA sequences, Eur. J. Biochem., 177:649–655.
Baron, M.D., Davison, M.D., Jones, P., and Critchley, D.R., 1987, The sequence of chicken actinin reveals homologies to spectrin and calmodulin. J. Biol. Chem., 36:17623–17629.
Bazari, W.L., Matsudaira, P., Wallek, M., Smeal, T., Jakes, R., and Ahmed, Y., 1988, Villin sequence and peptide map identify six homologous domains, Proc. Natl. Acad. Sci. USA. 85:4986–4990.
Bennett, J. P., Zaner, K.S., and Stossel, T.P., 1984, Isolation and some properties of macrophage actinin: Evidence that it is not an actin gelling protein. Biochemistry, 23:5081–5086.
Brown, S., Yamamoto, K., and Spudich, J.A., 1982, A 40,000-dalton protein from Dictyostelium discoideum affects assembly properties of actin in a Ca2+-dependent manner, J. Cell Biol., 93:205–210.
Koenig, M., Monaco, A.P., and Kunkel, L.M., 1988, The complete sequence of dystrophin predicts a rodshaped cytoskeletal protein, Cell, 53:219–228.
Kretsinger, R.H., 1980a, Structure and evolution of calcium modulated proteins. CRC Crit. Rev. Biochem., 8:119–174.
Kretsinger, R.H., 1980b, Crystallographic studies of calmodulin and homologs, Ann. NY Acad. Sci., 356:14–19.
Kwiatkowski, D., Stossel, T.D., Orkin, S.H., Mole, J.E., Colton, H.R., and Yin, H.L., 1986, Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature. 323:455–458.
Noegel, A., Witke, W., and Schleicher, M., 1987, Calcium-sensitive non-muscle actinin contains EF-hand structures and highly conserved regions. FEBS Lett., 221:391–396.
Noegel, A.A., and Schleicher, M., 1989, The contractile system in non-muscle cells: Involvement of actin and actin-binding proteins, In Stimulus-Response Coupling: The Role of Intracellular Calcium, J.R. Dedman and V.L. Smith, eds., Telford Press, in press.
Noegel, A.A., Rapp, S., Lottspeich, F., Schleicher, M., and Stewart, M., 1989, The Dictyostelium gelation factor shares a putative actin-binding site with actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation, J. Cell Biol., 109:607–618.
Pollard, T.D., and Cooper, J.A., 1986, Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Ann. Rev. Biochem., 55:987–1035.
Schleicher, M., Noegel, A., Schwarz, T., Wallraff, E., Brink, M., Faix, J., Gerisch, G., and Isenberg, G., 1988, A Dictyostelium mutant with severe defects in actinin: its characterization using cDNA probes and monoclonal antibodies. J. Cell Sci., 90:59–71.
Stossel, T.P., Chaponnier, C., Ezzell, R.M., Hartwig, J.H., Janmey, PA., Kwiatkowski, D.J., Lind, S.E., Smith, D.B., Southwick, F.S., Yin, H.L., and Zaner, K.S., 1985, Nonmuscle actin-binding proteins. Ann. Rev. Cell Biol., 1:353–402.
Tschudi, C., Young, A.S., Ruben, L., Patton, C.L., and Richards, F.F., 1985, Calmodulin genes in Trypanosomes are tandemly repeated and produce multiple mRNAs with a common 5’ leader sequence, Proc. Natl. Acad. Sci. USA, 82:3998–4002.
Wallraff, E., Schleicher, M., Modersitzki, M., Rieger, D., Isenberg, G., and Gerisch, G., 1986, Selection of Dictyostelium mutants defective in cytoskeletal proteins: use of an antibody that binds to the ends of actinin rods, EMBO J., 5:61–67.
Wasenius, V.-M., Saraste, M., Salven, P., Erämaa, M., Holms, L., and Lehto, V.P., 1989, Primary structure of the brain aspectrin. J. Cell Biol., 108:79–93.
Witke, W., Schleicher, M., Lottspeich, F., and Noegel, A., 1986, Studies on the transcription, translation, and structure of actinin in Dictyostelium discoideum. J. Cell Biol. 103:969–975.
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© 1990 Plenum Press, New York
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Schleicher, M., Eichinger, L., Witke, W., Noegel, A.A. (1990). Ca2+-Binding Proteins as Components of the Cytoskeleton. In: Pochet, R., Lawson, D.E.M., Heizmann, C.W. (eds) Calcium Binding Proteins in Normal and Transformed Cells. Advances in Experimental Medicine and Biology, vol 269. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5754-4_15
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DOI: https://doi.org/10.1007/978-1-4684-5754-4_15
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