Role of the basic C-terminal half of caldesmon in its regulation of F-actin: Comparison between caldesmon and calponin

Journal of Biochemistry

Volumn 138, Issue 6, 2005, Pages 805-813

  Takiguchi, Kingo ^a,b   Matsumura, Fumio ^a  

^a RUTGERS UNIVERSITY   (United States)

^b NAGOYA UNIVERSITY   (Japan)

Author keywords

Actin protection; Caldesmon; Calponin; Electrostatic interaction; Structure function relationship

Indexed keywords

CALDESMON; CALPONIN; F ACTIN; GELSOLIN; MYOSIN ADENOSINE TRIPHOSPHATASE; TROPOMYOSIN;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ELECTRICITY; NONHUMAN; PHOSPHORYLATION; RAT;

ACTINS; ANIMALS; CALCIUM-BINDING PROTEINS; CALMODULIN-BINDING PROTEINS; MICROFILAMENT PROTEINS; PROTEIN STRUCTURE, TERTIARY; RATS; STATIC ELECTRICITY;

ANIMALIA;

EID: 32944455600     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi181     Document Type: Article

References (56)

1. Yamashiro, S., Yamakita, Y., Hosoya, H., and Matsumura, F. (1991) Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis. Nature 349, 169-172
2. Yamashiro, S., Yamakita, Y., Yoshida, K., Takiguchi, K., and Matsumura, F. (1995) Characterization of the COOH terminus of non-muscle caldesmon mutants lacking mitosis-specific phosphorylation sites. J. Biol. Chem. 270, 4023-4030
3. Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc. Natl. Acad. Sci. USA 78, 5652-5655
4. Lash, J.A., Sellers, J.R., and Hathaway, D.R. (1986) The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin. J. Biol. Chem. 261, 16155-16160
5. Velaz, L., Hemric, M.E., Benson, C.E., and Chalovich, J.M. (1989) The binding of caldesmon to actin and its effect on the ATPase activity of soluble myosin subfragments in the presence and absence of tropomyosin. J. Biol. Chem. 264, 9602-9610
6. Shirinsky, V.P., Biryukov, K.G., Hettasch, J.M., and Sellers, J.R. (1992) Inhibition of the relative movement of actin and myosin by caldesmon and calponin. J. Biol. Chem. 267, 15886-15892
7. Fraser, I.D.C., and Marston, S.B. (1995) In vitro motility analysis of smooth muscle caldesmon control of actin-tropomyosin filament movement. J. Biol. Chem. 270, 19688-19693
8. Ikebe, M. and Reardon, S. (1988) Binding of caldesmon to smooth muscle myosin. J. Biol. Chem. 263, 3055-3058
9. Sutherland, C. and Walsh, M.P. (1989) Phosphorylation of caldesmon prevents its interaction with smooth muscle myosin. J. Biol. Chem. 264, 578-583
10. Marston, S.B. and Redwood, C.S. (1991) The molecular anatomy of caldesmon. Biochem. J. 279, 1-16
11. Sobue, K., Takahashi, K., and Wakabayash, I. (1985) Caldesmon150 regulates the tropomyosin-enhanced actin-myosin interaction in gizzard smooth muscle. Biochem. Biophys. Res. Commun. 132, 645-651
12. Horiuchi, K.Y., Miyata, H., and Chacko, S. (1986) Modulation of smooth muscle actomyosin ATPase by thin filament associated proteins. Biochem. Biophys. Res. Commun. 136, 962-968
13. Szpacenko, A. and Dabrowska, R. (1986) Functional domain of caldesmon. FEBS Lett. 202, 182-186
14. Ishikawa, R., Kagami, O., Hayashi, C., and Kohama, K. (1992) Characterization of smooth muscle caldesmon as a microtubule-associated protein. Cell Motil. Cytoskeleton 23, 244-251
15. Wang, C.L.A., Wang, L.W.C., Xu, S., Lu, R.C., Saavedra-Alanis, V., and Bryan, J. (1991) Localization of the calmodulin-and the actin-binding sites of caldesmon. J. Biol. Chem. 266, 9166-9172
16. Redwood, C.S. and Marston, S.B. (1993) Binding and regulatory properties of expressed functional domains of chicken gizzard smooth muscle caldesmon. J. Biol. Chem. 268, 10969-10976
17. Tsuruda, T.S., Watson, M.H., Foster, D.B., Lin, J.J., and Mak, A.S. (1995) Alignment of caldesmon on the actin-tropomyosin filaments. Biochem. J. 309, 951-957
18. Hayashi, K., Fujio, Y., Kato, I., and Sobue, K. (1991) Structural and functional relationships between h- and l-caldesmons. J. Biol. Chem. 266, 355-361
19. Horiuchi, K.Y., Samuel, M., and Chacko, S. (1991) Mechanism for the inhibition of acto-heavy meromyosin ATPase by the actin/calmodulin binding domain of caldesmon. Biochemistry 30, 712-717
20. Riseman, V.M., Lynch, W.P., Nefsky, B., and Bretscher, A. (1989) The calmodulin and F-actin binding sites of smooth muscle caldesmon lie in the carboxyl-terminal domain whereas the molecular weight heterogeneity lies in the middle of the molecule. J. Biol. Chem. 264, 2869-2875
21. Sobue, K. and Sellers, J.R. (1991) Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J. Biol. Chem. 266, 12115-12118
22. 2+. Potentiation of the annealing process by caldesmon. J. Biol. Chem. 264, 16764-16770
23. Gimona, M., Herzog, M., Vandekerckhove, J., and Small, J.V. (1990) Smooth muscle specific expression of calponin. FEBS Lett. 274, 159-162
24. Takahashi, K. and Nadal-Ginard, B. (1991) Molecular cloning and sequence analysis of smooth muscle calponin. J. Biol. Chem. 266, 13284-13288
25. Takahashi, K., Yoshimoto, R., Fuchibe, K., Fujishige, A., Mitsui-Saito, M., Hori, M., Ozaki, H., Yamamura, H., Awata, N., Taniguchi, S., Katsuki, M., Tsuchiya, T., and Karaki, H. (2000) Regulation of shortening velocity by calponin in intact contracting smooth muscles. Biochem. Biophys. Res. Commun. 279, 150-157
26. Winder, S.J. and Walsh, M.P. (1990) Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. J. Biol. Chem. 265, 10148-10155
27. Abe, M., Takahashi, K., and Hiwada, K. (1990) Effect of calponin on actin-activated myosin ATPase activity. J. Biochem. 108, 835-838
28. Winder, S.J. and Walsh, M.P. (1993) Calponin: thin filament-linked regulation of smooth muscle contraction. Cell. Signalling 5, 677-686
29. Makuch, R., Birukov, K., Shirinsky, V., and Dabrowska, R. (1991) Functional interrelationship between calponin and caldesmon. Biochem. J. 280, 33-38
30. Childs, T.J., Watson, M.H., Novy, R. E., Lin, J.J., and Mak, A.S. (1992) Calponin and tropomyosin interactions. Biochim. Biophys. Acta 1121, 41-46
31. Lin, Y., Ye, L.H., Ishikawa, R., Fujita, K., and Kohama, K. (1993) Stimulatory effect of calponin on myosin ATPase activity. J. Biochem. 113, 643-645
32. Borovikov, Yu. S., Horiuchi, K.Y., Avrova, S.V., and Chacko, S. (1996) Modulation of actin conformation and inhibition of actin filament velocity by calponin. Biochemistry 35, 13849-13857
33. 2+-regulated force in skinned smooth muscle of the rabbit mesenteric artery. Pflügers Arch. 427, 301-308
34. Winder, S.J., Allen, B.C., Fraser, E.D., Rang, H.-M., Kargacin, G.J., and Walsh, M.P. (1993) Calponin phosphorylation in vitro and in intact muscle. Biochem. J. 296, 827-836
35. Winder, S.J., Pato, M.D., and Walsh, M.P. (1992) Purification and characterization of calponin phosphatase from smooth muscle. Effect of dephosphorylation on calponin function. Biochem. J. 286, 197-203
36. Fraser, E.D. and Walsh, M.P. (1995) Dephosphorylation of calponin by type 2B protein phosphatase. Biochemistry 34, 9151-9158
37. Mino, T., Yuasa, U., Naka, M., and Tanaka, T. (1995) Phosphorylation of calponin mediated by protein kinase C in association with contraction in porcine coronary artery. Biochem. Biophys. Res. Commun. 208, 397-404
38. Kaneko, T., Amano, M., Maeda, A., Goto, H., Takahashi, K., Ito, M., and Kaibuchi, K. (2000) Identification of calponin as a novel substrate of Rho-kinase. Biochem. Biophys. Res. Commun. 273, 110-116
39. Gimona, M., Sparrow, M.P., Strasser, P., Herzog, M., and Small, J.V. (1992) Calponin and SM 22 isoforms in avian and mammalian smooth muscle. Absence of phosphorylation in vivo. Eur. J. Biochem. 205, 1067-1075
40. Bárány, M. and Bárány, K. (1993) Calponin phosphorylation does not accompany contraction of various smooth muscles. Biochim. Biophys. Acta 1179, 229-233
41. Adelstein, R.S. and Eisenberg, E. (1980) Regulation and kinetics of the actin-myosin-ATP interaction. Annu. Rev. Biochem. 49, 921-956
42. Hartshorne, D.J., Ito, M., and Erdodi, F. (1998) Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19, 325-341
43. Ishikawa, R., Yamashiro, S., and Matsumura, F. (1989) Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. J. Biol. Chem. 264, 7490-7497
44. Bretscher, A. (1984) Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties. J. Biol. Chem. 259, 12873-12880
45. Fujii, T., Imai, M., Rosenfeld, G.C., and Bryan, J. (1987) Domain mapping of chicken gizzard caldesmon. J. Biol. Chem. 262, 2757-2763
46. Takiguchi, K., Yamashiro-Matsumura, S., and Matsumura, F. (2000) Artificial phosphorylation removes Gelsolin's dependence on calcium. Cell Struct. Fund. 25, 57-65
47. Honda, M., Takiguchi, K., Ishikawa, S., and Hotani, H. (1999) Morphogenesis of liposomes encapsulating actin depends on the type of actin-crosslinking. J. Mol. Biol. 287, 293-300
48. Way, M., Gooch, J., Pope, B., and Weeds, A.G. (1989) Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109, 593-605
49. Chaponnier, C., Janmey, P.A., and Yin, H.L. (1986) The actin filament-severing domain of plasma gelsolin. J. Cell Biol. 103, 1473-1481
50. Sobue, K., Takahashi, K., Tanaka, T., Kanda, K., Ashino, N., Kakiuchi, S., and Maruyama, K. (1985) Crosslinking of actin filaments is caused by caldesmon aggregates, but not by its dimers. FEBS Lett. 182, 201-204
51. Lynch, W.P., Riseman, V.M., and Bretscher, A. (1987) Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sulfhydryl cross-linking. A mechanism for caldesmon's F-actin bundling activity. J. Biol. Chem. 262, 7429-7437
52. Harricane, M.C., Cavadore, C., Audemard, E., and Mornet, D. (1990) Complexes between 15 kDa caldesmon fragment and actin investigated by immune-electron microscopy. FEBS Lett. 269, 185-188
53. Tang, J.X. and Janmey, P.A. (1996) The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J. Biol. Chem. 271, 8556-8563
54. Moody, C., Lehman, W., and Craig, R. (1990) Caldesmon and the structure of smooth muscle thin filaments: electron microscopy of isolated thin filaments. J. Muscle Res. Cell Motil. 11, 176-185
55. Trabelsi-Terzidis, H., Fattoum, A., Represa, A., Dessi, F., Ben-Ari, Y., and der Terrossian, E. (1995) Expression of an acidic isoform of calponin in rat brain: western blots on one-or two-dimensional gels and immunolocalization in cultured cells. Biochem. J. 15, 211-215
56. Matthew, J.D., Khromov, A.S., McDuffie, M.J., Somlyo, A.V., Somlyo, A.P., Taniguchi, S., and Takahashi, K. (2000) Contractile properties and proteins of smooth muscles of a calponin knockout mouse. J. Physiol. 529, 811-824