Ca2+-Binding Proteins as Components of the Cytoskeleton

  • Michael Schleicher
  • Ludwig Eichinger
  • Walter Witke
  • Angelika A. Noegel
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)


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.


Dictyostelium Discoideum Chicken Brain 42bp Oligonucleotide Chicken Fibroblast Brain Spectrin 
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  1. 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.Google Scholar
  2. 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.PubMedGoogle Scholar
  3. 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.PubMedCrossRefGoogle Scholar
  4. 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.Google Scholar
  5. 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.PubMedCrossRefGoogle Scholar
  6. 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.PubMedCrossRefGoogle Scholar
  7. 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.PubMedCrossRefGoogle Scholar
  8. Koenig, M., Monaco, A.P., and Kunkel, L.M., 1988, The complete sequence of dystrophin predicts a rodshaped cytoskeletal protein, Cell, 53:219–228.PubMedCrossRefGoogle Scholar
  9. Kretsinger, R.H., 1980a, Structure and evolution of calcium modulated proteins. CRC Crit. Rev. Biochem., 8:119–174.PubMedCrossRefGoogle Scholar
  10. Kretsinger, R.H., 1980b, Crystallographic studies of calmodulin and homologs, Ann. NY Acad. Sci., 356:14–19.PubMedCrossRefGoogle Scholar
  11. 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.PubMedCrossRefGoogle Scholar
  12. 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.PubMedCrossRefGoogle Scholar
  13. 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.Google Scholar
  14. 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.PubMedCrossRefGoogle Scholar
  15. 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.PubMedCrossRefGoogle Scholar
  16. 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.PubMedGoogle Scholar
  17. 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.PubMedCrossRefGoogle Scholar
  18. 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.PubMedCrossRefGoogle Scholar
  19. 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.PubMedGoogle Scholar
  20. 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.PubMedCrossRefGoogle Scholar
  21. 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.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Michael Schleicher
    • 1
  • Ludwig Eichinger
    • 1
  • Walter Witke
    • 1
  • Angelika A. Noegel
    • 1
  1. 1.Max-Planck-Institute for BiochemistryMartinsriedGermany

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