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Gene Review

CALD1  -  caldesmon 1

Gallus gallus

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Disease relevance of CALD1


High impact information on CALD1


Biological context of CALD1


Anatomical context of CALD1


Associations of CALD1 with chemical compounds

  • Two isoforms of caldesmon conserve the completely identical sequences in the NH2- and COOH-terminal domains except for the insertion of Ala-508 in l-caldesmon [8].
  • Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex [10].
  • Mitosis-specific phosphorylation by cdc2 kinase causes nonmuscle caldesmon to dissociate from microfilaments (Yamashiro, S., Yamakita, Y., Ishikawa, R., and Matsumura, F. (1990) Nature 344, 675-678; Yamashiro, S., Yamakita, Y., Hosoya, H., and Matsumura, F. (1991) Nature 349, 169-172) [7].
  • To identify the tyrosine phosphorylation site(s) in the CaD molecule and to further elucidate the functional role of CaD tyrosine phosphorylation in S3-v-ErbB oncogenic signaling, we have generated a series of mutant CaDs in which one or more tyrosine residues have been replaced with phenylalanine [10].
  • Carbodiimide crosslinking with actin revealed that the 15kDa part of the molecule is probably not involved in the actin binding process but may participate in a twisting of the F-actin filament and be responsible of the caldesmon regulatory function during smooth muscle contraction [13].

Physical interactions of CALD1


Enzymatic interactions of CALD1


Regulatory relationships of CALD1


Other interactions of CALD1


Analytical, diagnostic and therapeutic context of CALD1


  1. Primary structure and functional expression of h-caldesmon complementary DNA. Hayashi, K., Kanda, K., Kimizuka, F., Kato, I., Sobue, K. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  2. Heat treatment could affect the biochemical properties of caldesmon. Zhuang, S., Mabuchi, K., Wang, C.A. J. Biol. Chem. (1996) [Pubmed]
  3. Characterization of the autophosphorylation of chicken gizzard caldesmon. Scott-Woo, G.C., Walsh, M.P. Biochem. J. (1988) [Pubmed]
  4. Immunodetection and intracellular localization of caldesmon-like proteins in Amoeba proteus. Gagola, M., Kłopocka, W., Greebecki, A., Makuch, R. Protoplasma (2003) [Pubmed]
  5. Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments. Vibert, P., Craig, R., Lehman, W. J. Cell Biol. (1993) [Pubmed]
  6. Microinjection of nonmuscle and smooth muscle caldesmon into fibroblasts and muscle cells. Yamakita, Y., Yamashiro, S., Matsumura, F. J. Cell Biol. (1990) [Pubmed]
  7. Characterization of mitotically phosphorylated caldesmon. Yamakita, Y., Yamashiro, S., Matsumura, F. J. Biol. Chem. (1992) [Pubmed]
  8. Structural and functional relationships between h- and l-caldesmons. Hayashi, K., Fujio, Y., Kato, I., Sobue, K. J. Biol. Chem. (1991) [Pubmed]
  9. Cloning and expression of a smooth muscle caldesmon. Bryan, J., Imai, M., Lee, R., Moore, P., Cook, R.G., Lin, W.G. J. Biol. Chem. (1989) [Pubmed]
  10. Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex. Wang, Z., Danielsen, A.J., Maihle, N.J., McManus, M.J. J. Biol. Chem. (1999) [Pubmed]
  11. 35 kDa fragment of h-caldesmon conserves two consensus sequences of the tropomyosin-binding domain in troponin T. Hayashi, K., Yamada, S., Kanda, K., Kimizuka, F., Kato, I., Sobue, K. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  12. Identification of two distinct promoters in the chicken caldesmon gene. Yano, H., Hayashi, K., Haruna, M., Sobue, K. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  13. Identification of a 15 kilodalton actin binding region on gizzard caldesmon probed by chemical cross-linking. Mornet, D., Audemard, E., Derancourt, J. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  14. Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity. Wang, Z., Jiang, H., Yang, Z.Q., Chacko, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  15. The role of tropomyosin in the interactions of F-actin with caldesmon and actin-binding protein (or filamin). Nomura, M., Yoshikawa, K., Tanaka, T., Sobue, K., Maruyama, K. Eur. J. Biochem. (1987) [Pubmed]
  16. Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon. Hemric, M.E., Lu, F.W., Shrager, R., Carey, J., Chalovich, J.M. J. Biol. Chem. (1993) [Pubmed]
  17. Evidence against the regulation of caldesmon inhibitory activity by p42/p44erk mitogen-activated protein kinase in vitro and demonstration of another caldesmon kinase in intact gizzard smooth muscle. Krymsky, M.A., Chibalina, M.V., Shirinsky, V.P., Marston, S.B., Vorotnikov, A.V. FEBS Lett. (1999) [Pubmed]
  18. Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles. Pfitzer, G., Zeugner, C., Troschka, M., Chalovich, J.M. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  19. Calcium-dependent regulation of interactions of caldesmon with calcium-binding proteins found in growth cones of chick forebrain neurons. Alexanian, A.R., Bamburg, J.R., Hidaka, H., Mornet, D. Cell. Mol. Neurobiol. (2001) [Pubmed]
  20. Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties. Bretscher, A. J. Biol. Chem. (1984) [Pubmed]
  21. Caldesmon-binding sites on tropomyosin. Watson, M.H., Kuhn, A.E., Novy, R.E., Lin, J.J., Mak, A.S. J. Biol. Chem. (1990) [Pubmed]
  22. Reconstitution of Ca2+-sensitive gelation of actin filaments with filamin, caldesmon and calmodulin. Sobue, K., Morimoto, K., Kanda, K., Maruyama, K., Kakiuchi, S. FEBS Lett. (1982) [Pubmed]
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