Journal of Muscle Research & Cell Motility

, Volume 18, Issue 1, pp 1–16 | Cite as

Myosin light chain kinases

  • PATRICIA J. GALLAGHER
  • B. PAUL HERRING
  • JAMES T. STULL

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References

  1. ALESSI, D., MACDOUGALL, L. K., SOLA, M. M., IKEBE, M. & COHEN, P. (1992) The control of protein phosphatase-1 by targeting subunits. Eur. J. Biochem. 210, 1023–35.PubMedCrossRefGoogle Scholar
  2. BABIYCHUK, E. B., BABIYCHUK, V. S. & SOBIESZEK, A. (1995) Modulation of smooth muscle myosin light chain kinase activity by Ca2+/calmodulin-dependent, oligomeric-type modifications. Biochemistry 34, 6366–72.PubMedCrossRefGoogle Scholar
  3. BAGCHI, I. C., KEMP, B. E. & MEANS, A. R. (1989) Myosin light chain kinase structure function analysis using bacterial expression. J. Biol. Chem. 264, 15843–9.PubMedGoogle Scholar
  4. BAGCHI, I. C., HUANG, Q. & MEANS, A. R. (1992a) Identification of amino acids essential for calmodulin binding and activation of smooth muscle myosin light chain kinase. J. Biol. Chem. 267, 3024–9.PubMedGoogle Scholar
  5. BAGCHI, I. C., KEMP, B. E. & MEANS, A. R. (1992b) Intrasteric regulation of myosin light chain kinase: The pseudosubstrate prototope binds to the active site. Mol. Endocrinol. 6, 621–6.PubMedCrossRefGoogle Scholar
  6. BLUMENTHAL, D. K., TAKIO, K., EDELMAN, A. M., CHARBONNEAU, H., TITANI, K., WALSH, K. A. & KREBS, E. G. (1985) Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Proc. Natl Acad. Sci. USA 82, 3187–91.PubMedCrossRefGoogle Scholar
  7. BOWMAN, B. F., PETERSON, J. A., & STULL, J. T. (1992) Presteady-state kinetics of the activation of rabbit skeletal muscle myosin light chain kinase by Ca2+/calmodulin. J. Biol. Chem. 267, 5346–54.PubMedGoogle Scholar
  8. CAMPBELL, I. D. & SPITZFADEN, C. (1994) Building proteins with fibronectin type III modules. Structure 2, 333–7.PubMedCrossRefGoogle Scholar
  9. CARAFOLI, E. (1991) Calcium pump of the plasma membrane. Physiol. Rev. 71, 129–53.PubMedGoogle Scholar
  10. CHOI, O. H., ADELSTEIN, R. S. & BEAVEN, M. A. (1994) Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C. J. Biol. Chem. 269, 536–41.PubMedGoogle Scholar
  11. COLBURN, J. C., MICHNOFF, C. H., HSU, L., SLAUGHTER, C. A., KAMM, K. E. & STULL, J. T. (1988) Sites phosphorylated in myosin light chain in contracting smooth muscle. J. Biol. Chem. 263, 19166–73.PubMedGoogle Scholar
  12. COLLINGE, M., MATRISIAN, P. E., ZIMMER, W. E., SHATTUCK, R. L., LUKAS, T. J., VAN ELDIK, L. J. & WATTERSON, D. M. (1992) Structure and expression of a calcium-binding protein gene contained within a calmodulin-regulated protein kinase gene. Mol. Cell. Biol. 12, 2359–71.PubMedGoogle Scholar
  13. CONTI, M. A. & ALDELSTEIN, R. S. (1981) The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3·.5· cAMP-dependent protein kinase. J. Biol. Chem. 256, 3178–81.PubMedGoogle Scholar
  14. CORSON, M. A., SELLERS, J. R., ADELSTEIN, R. S. & SCHOENBERG, M. (1990) Substance P contracts bovine tracheal smooth muscle via activation of myosin light chain kinase. Am. J. Physiol. 259, C258–65.Google Scholar
  15. DE LANEROLLE, P., ADELSTEIN, R. S., FERAMISCO, J. R. & BURRIDGE, K. (1981) Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells. Proc. Natl Acad. Sci. USA 78, 4738–42.PubMedCrossRefGoogle Scholar
  16. DE LANEROLLE, P, NISHIKAWA, M., YOST, D. A. & ADELSTEIN, R. S. (1984) Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle. Science 223, 1415–17.PubMedGoogle Scholar
  17. DE LANEROLLE, P., NISHIKAWA, M., FELSEN, R. & ADELSTEIN, R. S. (1987) Immunological properties of myosin light-chain kinases. Biochim. Biophys. Acta 914, 74–82.PubMedGoogle Scholar
  18. DENT, P., MACDOUGALL, L. K., MACKINTOSH, C., CAMPBELL, D. G. & COHEN, P. (1992) A myofibrillar protein phosphatase from rabbit skeletal muscle contains the β isoform of protein phosphatase-1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin. Eur. J. Biochem. 210, 1037–44.PubMedCrossRefGoogle Scholar
  19. EDELMAN, A. M., TAKIO, BLUMENTHAL, D. K., HANSEN, R. S., WALSH, K. A., TITANI, K. & KREBS, E. G. (1985) Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. J. Biol. Chem. 260, 11275–85.PubMedGoogle Scholar
  20. FINDLAY, W. A., GRADWELL, M. J. & BAYLEY, P. M. (1995) Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin. Protein Sci. 4, 2375–82.PubMedCrossRefGoogle Scholar
  21. FISHER, S. A. & IKEBE, M. (1995) Developmental and tissue distribution of expression of nonmuscle and smooth muscle isoforms of myosin light chain kinase. Biochem. Biophys. Res. Commun. 217, 696–703.PubMedCrossRefGoogle Scholar
  22. FITZSIMONS, D. P., HERRING, B. P., STULL, J. T. & GALLAGHER, P. J. (1992) Identification of basic residues involved in activation and calmodulin binding of rabbit smooth muscle myosin light chain kinase. J. Biol. Chem. 267, 23903–9.PubMedGoogle Scholar
  23. FOYT, H. L., GUERRIERO, V., JR. & MEANS, A. R. (1985) Functional domains of chicken gizzard myosin light chain kinase. J. Biol. Chem. 260, 7765–74.PubMedGoogle Scholar
  24. GALLAGHER, P. J. & HERRING, B. P. (1991) The C-terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin. J. Biol. Chem. 266, 23945–52.PubMedGoogle Scholar
  25. GALLAGHER, P. J., HERRING, B. P., GRIFFIN, S. A. & STULL, J. T. (1991) Molecular characterization of a mammalian smooth muscle myosin light chain kinase. J. Biol. Chem. 266, 23936–44.PubMedGoogle Scholar
  26. GALLAGHER, P. J., HERRING, B. P., TRAFNY, A., SOWADSKI, J. & STULL, J. T. (1993) A molecular mechanism for autoinhibition of myosin light chain kinases. J. Biol. Chem. 268, 26578–82.Google Scholar
  27. GALLAGHER, P. J., HERRING, B. P., TRAFNY, A., SOWADSKI, J. & STULL, J. T. (1994) A molecular mechanism for autoinhibition of myosin light chain kinases. J. Biol. Chem. 269, 26578–82.Google Scholar
  28. GALLAGHER, P. J., GARCIA, J. G. N. & HERRING, B. P. (1995) Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells. J. Biol. Chem. 270, 29090–5.PubMedCrossRefGoogle Scholar
  29. GAO, Z. H., KREBS, J., VANBERKUM, M. F. A., TANG, W.-J., MAUNE, J. F., MEANS, A. R., STULL, J. T. & BECKINGHAM, K. (1993) Activation of four enzymes by two series of calmodulin mutants with point mutations in individual Ca2+ binding sites. J. Biol. Chem. 268, 20096–104.PubMedGoogle Scholar
  30. GAO, Z.-H., ZHI, G., HERRING, B. P., MOOMAW, C., DEOGNY, L., SLAUGHTER, C. A. & STULL, J. T. (1995) Photoaffinity labeling of a peptide substrate to myosin light chain kinase. J. Biol. Chem. 270, 10125–35.PubMedCrossRefGoogle Scholar
  31. GARCIA, J. G. N., DAVIS, H. W. & PATTERSON, C. E. (1995) Regulation of endothelial cell gap formation and barrier dysfunction: role of myosin light chain phosphorylation. J. Cell. Physiol. 163, 510–22.PubMedCrossRefGoogle Scholar
  32. GAUTEL, M., CASTIGLIONE-MORELLI, M. A., PFUHL, M., MOTTA, A. & PASTORE, A. (1995) A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase. Eur. J. Biochem. 230, 752–9.PubMedCrossRefGoogle Scholar
  33. GEUSS, U., MAYR, G. W. & HEILMAYER, L. M. G., JR. (1985) Steady-state kinetics of skeletal muscle myosin light chain kinase indicate a strong down regulation by products. Eur. J. Biochem. 153, 327–34.PubMedCrossRefGoogle Scholar
  34. GOECKELER, Z. M. & WYSOLMERSKI, R. B. (1995) Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, actin polymerization, and myosin phosphorylation. J. Cell Biol. 130, 613–27.PubMedCrossRefGoogle Scholar
  35. GOLDBERG, J., NAIRN, A. C. & KURIYAN, J. (1996) Structural basis for the autoinhibition of calcium/ calmodulin-dependent protein kinase I. Cell 84, 887.CrossRefGoogle Scholar
  36. GRIFFITH, L. M., DOWNS, S. M. & SPUDICH, J. A. (1987) Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function. J. Cell Biol. 104, 1309–23.PubMedCrossRefGoogle Scholar
  37. GUERRIERO, V., JR., ROWLEY, D. R. & MEANS, A. R. (1981) Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. Cell 27, 449–58.PubMedCrossRefGoogle Scholar
  38. HARTSHORNE, D. J. (1987) Biochemistry of the contractile process in smooth muscle. In Physiology of the Gastrointestinal Tract (edited by JOHNSON, L. R.) pp. 423–82. New York: Raven Press.Google Scholar
  39. HASHIMOTO, Y. & SODERLING, T. R. (1990) Phosphorylation of smooth muscle myosin light chain kinase by Ca2+/calmodulin-dependent protein kinase-II. Comparative study of the phosphorylation sites. Arch. Biochem. Biophys. 278, 41–5.PubMedCrossRefGoogle Scholar
  40. HASHIMOTO, Y., SASAKI, H., TOGO, M., TSUKAMOTO, K. HORIE, Y., FUKATA, H., WATANABE, T. & KUROKASA, K. (1994) Roles of myosin light-chain kinase in platelet shape change and aggregation. Biochim. Biophys. Acta 1223, 163–9.PubMedCrossRefGoogle Scholar
  41. HEIERHORST, J., PROBST, W. C., VILIM, F. S., BUKU, A. & WEISS, K. R. (1994) Autophosphorylation of molluscan twitchin and interaction of its kinase domain with calcium/calmodulin. J. Biol. Chem. 269, 21086–93.PubMedGoogle Scholar
  42. HEIERHORST, J., PROBST, W. C., KOHANSKI, R. A., BUKU, A. & WEISS, K. R. (1995) Phosphorylation of myosin regulation light chains by the molluscan twitchin kinase. Eur. J. Biochem. 233, 426–31.PubMedCrossRefGoogle Scholar
  43. HEIERHORST, J., KOBE, B., FEIL, S. C., PARKER, M. W., BENIAN, G. M., WEISS, K. R. & KEMP, B. E. (1996) Ca2+/S100 regulation of giant protein kinases. Nature 380, 636–9.PubMedCrossRefGoogle Scholar
  44. HERRING, B. P. (1991) Basic residues are important for Ca2+/calmodulin binding and activation but not autoinhibition of rabbit skeletal muscle myosin light chain kinase. J. Biol. Chem. 266, 11838–41.Google Scholar
  45. HERRING, B. P. (1994) Smooth muscle MLCK expression in skeletal and cardiac muscle: functional implications. J. Cell. Biochem.(Supplement 18D), 509 (Abstract).Google Scholar
  46. HERRING, B. P. & SMITH, A. F. (1996) Telokin expression is mediated by a smooth muscle cell-specific promoter. Am. J. Physiol., in press.Google Scholar
  47. HERRING, B. P., NUNNALLY, M. H. GALLAGHER, P. J. & STULL, J. T. (1989) Molecular characterization of rat skeletal muscle myosin light chain kinase. Am. J. Physiol. 256, C399–404.Google Scholar
  48. HERRING, B. P., STULL, J. T. & GALLAGHER, P. J. (1990) Domain characterization of rabbit skeletal muscle myosin light chain kinase. J. Biol. Chem. 265, 1724–30.PubMedGoogle Scholar
  49. HOLDEN, H. M., ITO, M., HARTSHORNE, D. J. & RAYMENT, I. (1992) X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 Å resolution. J. Mol. Biol. 227, 840–51.PubMedCrossRefGoogle Scholar
  50. HU, S.-H., PARKER, M. W., LEL, J. Y., WILCE, M. C. J., BENIAN, G. M. & KEMP, B. E. (1994) Insights into autoregulation from the crystal structure of twitchin kinase. Nature 369, 581–4.PubMedCrossRefGoogle Scholar
  51. IKEBE, M. & REARDON, S. (1990) Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase. J. Biol. Chem. 265, 8975–8.PubMedGoogle Scholar
  52. IKEBE, M., MARUTA, S. & REARDON, S. (1989) Location of the inhibitory region of smooth muscle myosin light chain kinase. J. Biol. Chem. 264, 6967–71.PubMedGoogle Scholar
  53. IKEBE, M., IKEBE, R., KAMISOYAMA, H., REARDON, S., SCHWONEK, J. P., SANDERS, C. R., II & MATSURRA, M. (1994) Function of the NH2-terminal domain of the regulatory light chain on the regulation of smooth muscle myosin. J. Biol. Chem. 269, 28173–80.Google Scholar
  54. IKURA, M., CLORE, G. M., GRONENBORN, A. M., ZHU, G., KLEE, C. B. & BAX, A. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632–8.PubMedGoogle Scholar
  55. ITO, M., DABROWSKA, R., GUERRIERO, V., JR. & HARTSHORNE, D. J. (1989) Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain. J. Biol. Chem. 264, 13971–4.PubMedGoogle Scholar
  56. ITO, M., GUERRIERO, V., JR, CHEN, X. & HARTSHORNE, D. J. (1991) Definition of the inhibitory domain of smooth muscle mysoin light chain kinase by site-directed mutagenesis. Biochemistry 30, 3498–503.PubMedCrossRefGoogle Scholar
  57. JOHNSON, J. D., HOLROYDE, M. J., CROUCH, T. H., SOLARO, R. J. & POTTER, J. D. (1981) Fluorescence studies of the interaction of calmodulin with myosin light chain kinase. J. Biol. Chem. 256, 12194–8.PubMedGoogle Scholar
  58. JOHNSON, J. D., SNYDER, C., WALSH, M. & FLYNN, M. (1996) Effects of myosin light chain kinase and peptides on Ca2+ exchange with the N-and C-terminal Ca2+ binding sites of calmodulin. J. Biol. Chem. 271, 761–7.PubMedCrossRefGoogle Scholar
  59. KAMM, K. E. & GRANGE, R. W. (1996) Ca2+ sensitivity of contraction. In Biochemistry of Smooth Muscle Contraction (edited by BARANY, M.) pp. 355–65. Orlando: Academic Press.Google Scholar
  60. KAMM, K. E. & STULL, J. T. (1985) The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25, 593–620.PubMedCrossRefGoogle Scholar
  61. KAMM, K. E., HSU, L.-C., KUBOTA, Y. & STULL, J. T. (1989) Phosphorylation of smooth muscle myosin heavy and light chains: effects of phorbol dibutyrate and agonists. J. Biol. Chem. 264, 21223–9.PubMedGoogle Scholar
  62. KANOH, S., ITO, M., NIWA, E., KAWANO, Y. & HARTSHORNE, D. J. (1993) Actin-binding peptide from smooth muscle myosin light chain kinase. Biochemistry 32, 8902–7.PubMedCrossRefGoogle Scholar
  63. KASTURI, R., VASULKA, C. & JOHNSON, J. D. (1993) Ca2+, calmodulin, and myosin light chain kinase exchange with calmodulin. J. Biol. Chem. 268, 7958–64.PubMedGoogle Scholar
  64. KAWAMOTO, S., BENGUR, A. R., SELLERS, J. R. & ADELSTEIN, R. S. (1989) In situphosphorylation of human platelet myosin heavy and light chains by protein kinase C. J. Biol. Chem. 264, 2258–65.PubMedGoogle Scholar
  65. KELLER, T. C. S., III (1995) Structure and function of titin and nebulin. Curr. Biol. 7, 32–8.CrossRefGoogle Scholar
  66. KEMP, B. E. & PEARSON, R. B. (1991) Intrasteric regulation of protein kinases and phosphatases. Biochim. Biophys. Acta 1094, 67–76.PubMedCrossRefGoogle Scholar
  67. KEMP, B. E, PEARSON, R. B. & HOUSE, C. (1983) Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase. Proc. Natl Acad. Sci. USA 80, 7471–5.PubMedCrossRefGoogle Scholar
  68. KEMP, B. E., PEARSON, R. B., GUERRIERO, V., JR, BAGCHI, I. C. & MEANS, A. R. (1987) The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. J. Biol. Chem. 262, 2542–8.PubMedGoogle Scholar
  69. KEMP, B. E., FAUX, M. C., MEANS, A. R., HOUSE, C., TIGANIS, T., HU, S.-H. & MITCHELHILL, K. I. (1994) Structural aspects: pseudosubstrate and substrate interactions. In Protein Kinases (edited by WOODGETT, J. R.) pp. 30–67. Oxford: IRL Press.Google Scholar
  70. KENNELLY, P. J., COLBURN, J. C., LORENZEN, J., EDELMAN, A. M., STULL, J. T. & KREBS, E. G. (1991) Activation mechanism of rabbit skeletal muscle myosin light chain kinase. 5·-p-fluorosulfonylbenzoyl adenosine as a probe of the MgATP-binding site of the calmodulin-bound and calmodulin-free enzyme. FEBS Letts 286, 217–20.CrossRefGoogle Scholar
  71. KENNELLY, P. J., LENG, J. & MARCHAND, P. (1992) The MgATP-binding site on chicken gizzard myosin light chain kinase remains open and functionally competent during the calmodulin-dependent activation-inactivation cycle of the enzyme. Biochemistry 31, 5394–9.PubMedCrossRefGoogle Scholar
  72. KERRICK, W. G. L. & BOURGUIGNON, L. Y. (1984) Regulation of receptor capping in mouse lymphoma T cells by Ca2+-activated myosin light chain kinase. Proc. Natl Acad. Sci. USA 81, 165–9.PubMedCrossRefGoogle Scholar
  73. KIMURA, E., MATSUURA, I., TAI, K., NAKASHIMA, K.-I., & YAZAWA, M. (1994) The C-terminal half-molecular domain of calmodulin is responsible for high-affiinity interaction with target enzymes. Proc. Japan Acad. 71, 293–8.Google Scholar
  74. KNIGHTON, D. R., ZHENG, J. H., TEN EYCK, L. F., XUONG, N. H., TAYLOR, S. S. & SOWADSKI, J. M. (1991) Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414–20.PubMedGoogle Scholar
  75. KNIGHTON, D. R., PEARSON, R. B., SOWADSKI, J. M., MEANS, A. R., TEN EYCK, L. F., TAYLOR, S. S. & KEMP, B. E. (1992) Structural basis of the intrasteric regulation of myosin light chain kinases. Science 258, 130–5.PubMedGoogle Scholar
  76. KOBAYASHI, H., INOUE, A., MIKAWA, T., KUWAYAMA, H., HOTTA, Y., MASAKI, T. & EBASHI, S. (1992) Isolation of cDNA for bovine stomach 155 kDa protein exhibiting myosin light chain kinase activity. J. Biochem. 112, 786–91.PubMedGoogle Scholar
  77. KOLODNEY, M. S. & ELSON, E. L. (1995) Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain. Proc. Natl Acad. Sci. USA 92, 10252–6.PubMedCrossRefGoogle Scholar
  78. KREBS, E. G. & BEAVO, J. A. (1979) Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48, 923–59.PubMedCrossRefGoogle Scholar
  79. KRUEGER, J. K., PADRE, R. C. & STULL, J. T. (1995) Intrasteric regulation of myosin light chain kinase. J. Biol. Chem. 270, 16848–53.PubMedCrossRefGoogle Scholar
  80. LABEIT, S. & KOLMERER, B. (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293–6.Google Scholar
  81. LEACHMAN, S. A., GALLAGHER, P. J., HERRING, B. P., MCPHAUL, M. J. & STULL, J. T. (1992) Biochemical properties of chimeric skeletal and smooth muscle myosin light chain kinase. J. Biol. Chem. 267, 4930–8.PubMedGoogle Scholar
  82. LEI, J., TANG, X., CHAMBERS, T. C., POHL, J. & BENIAN, G. M. (1994) Protein kinase domain of twitchin has protein kinase activity and an autoinhibitory region. J. Biol. Chem. 269, 21078–85.Google Scholar
  83. LUBY-PHELPS, K., LANNI, F. & TAYLOR, D. L. (1985) Behavior of a fluorescent analogue of calmodulin in living 3T3 cells. J. Cell Biol. 101, 1245–56.PubMedCrossRefGoogle Scholar
  84. LUDOWYKE, R. I., PELEG, I., BEAVEN, M. A. & ADELSTEIN, R. S. (1989) Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells. J. Biol. Chem. 264, 12492–501.PubMedGoogle Scholar
  85. LUKAS, T. J., BURGESS, W. H., PRENDERGAST, F. G., LAU, W. & WATTERSON, D. M. (1986) Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. Biochemistry 25, 1458–64.PubMedCrossRefGoogle Scholar
  86. LUKAS, T. J., COLLINGE, M., HAIECH, J. & WATTERSON, D. M. (1994) Gain of function mutations for yeast calmodulin and calcium dependent regualtion of protein kinase activity. Biochim. Biophys. Acta 1223, 341–7.PubMedCrossRefGoogle Scholar
  87. MAMIYA, S., HAGIWARA, M., INOUE, S. & HIDAKA, H. (1989) Thyroid hormones inhibit platelet function and myosin light chain kinase. J. Biol. Chem. 264, 8575–9.PubMedGoogle Scholar
  88. MARUYAMA, K. (1994) Connectin, an elastic protein of striated muscle. Biophys. Chem. 50, 73–85.PubMedCrossRefGoogle Scholar
  89. MATSUSHIMA, S., HUANG, Y. P., DUDAS, C. V., GUERRIERO, V., JR. & HARTSHORNE, D. J. (1994) Mutants of smooth muscle myosin light chain kinase at tryptophan 800. Biochem. Biophys. Res. Commun. 202, 1329–36.PubMedCrossRefGoogle Scholar
  90. MEADOR, W. E., MEANS, A. R. & QUIOCHO, F. A. (1992) Target enzyme recognition by calmodulin: 2.4 A° structure of a calmodulin-peptide complex. Science 257, 1251–5.PubMedGoogle Scholar
  91. MICHNOFF, C. H., KEMP, B. E. & STULL, J. T. (1986) Phosphorylation of synthetic peptides by skeletal muscle myosin light chain kinases. J. Biol. Chem. 261, 8320–6.PubMedGoogle Scholar
  92. MILLER, J. R., SILVER, P. J. & STULL, J. T. (1983) The role of myosin light chain kinase phosphorylation in β-adrenergic relaxation of tracheal smooth muscle. Mol. Pharmacol. 24, 235–42.PubMedGoogle Scholar
  93. MILLER-HANCE, W. C., MILLER, J. R., WELLS, J. N., STULL, J. T. & KAMM, K. E. (1988) Biochemical events associated with activation of smooth muscle contraction. J. Biol. Chem. 263, 13979–82.PubMedGoogle Scholar
  94. NAKA, M., NISHIKAWA, M., ADELSTEIN, R. S. & HIDAKA, H. (1983) Phorbol ester-induced activation of human platelets is associated with protein kinase C phosphorylation of myosin light chains. Nature 306, 490–2.PubMedCrossRefGoogle Scholar
  95. NAKASHIMA, K-I., MAEKAWA, H. & YAZAWA, M. (1996) Chimeras of yeast and chicken calmodulin demonstrate differences in activation mechanisms of target enzymes. Biochemistry 35, 5602–10.PubMedCrossRefGoogle Scholar
  96. NISHIKAWA, M., HIDAKA, H. & ADELSTEIN, R. S. (1983) Phosphorylation of smooth muscle heavy meromyosin by calcium-activated, phospholipid-dependent protein kinase. The effect on actin-activated MgATPase activity. J. Biol. Chem. 258, 14069–72.PubMedGoogle Scholar
  97. NOMURA, M., STULL, J. T., KAMM, K. E. & MUMBY, M. C. (1992) Site-specific dephosphorylation of smooth muscle myosin light chain kinase by protein phosphatases 1 and 2A. Biochemistry 31, 11915–20.PubMedCrossRefGoogle Scholar
  98. OLSON, N. J., PEARSON, R. B., NEEDLEMAN, D. S., HURWITZ, M. Y., KEMP, B. E. & MEANS, A. R. (1990) Regulatory and structural motifs of chicken gizzard myosin light chain kinase. Proc. Natl Acad. Sci. USA 87, 2284–8.PubMedCrossRefGoogle Scholar
  99. O'NEIL, K. T. & DEGRADO, W. F. (1990) How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices. Trends Biochem. Sci. 15, 59–63.PubMedCrossRefGoogle Scholar
  100. PATO, M. D. & ADELSTEIN, R. S. (1983) Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation. J. Biol. Chem. 258, 7047–54.PubMedGoogle Scholar
  101. PEARSON, R. B., MISCONI, L. Y. & KEMP, B. E. (1986) Smooth muscle myosin kinase requires residues on the COOH-terminal side of the phosphorylation site. Peptide inhibitors. J. Biol. Chem. 261, 25–7.PubMedGoogle Scholar
  102. PEARSON, R. B., WETTENHALL, R. E. H., MEANS, A. R., HARTSHORNE, D. J. & KEMP, B. E. (1988) Autoregulation of enzymes by pseudosubstrate prototopes: myosin light chain kinase. Science 241, 970–3.PubMedGoogle Scholar
  103. PERSECHINI, A., MCMILLAN, K. & LEAKEY, P. (1994) Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments. J. Biol. Chem. 269, 16148–54.PubMedGoogle Scholar
  104. PERSECHINI, A., GANSZ, K. J. & PARESI, R. J. (1996) Activation of myosin light chain kinase and nitric oxide synthase activities by engineered calmodulins with duplicated or exchanged EF hand pairs. Biochemistry 35, 224–8.PubMedCrossRefGoogle Scholar
  105. POTIER, M.-C., CHELOT, E., PEKARSKY, Y., GARDINER, K., ROSSIER, J. & TURNELL, W. G. (1995) The human myosin light chain kinase (MLCK) from hippocampus: cloning, sequencing, expression, and localization to 3qcen-q21. Genomics 29, 562–70.PubMedCrossRefGoogle Scholar
  106. ROUSH, C. L., KENNELLY, P. J., GLACCUM, M. B., HELFMAN, D. M., SCOTT, J. D. & KREBS, E. G. (1988) Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. Sequence and tissue distribution. J. Biol. Chem. 263, 10510–16.PubMedGoogle Scholar
  107. RÜEGG, J. C., PFITZER, G., ZIMMER, M. & HOFMANN, F. (1984) The calmodulin fraction responsible for contraction in an intestinal smooth muscle. FEBS Letts 170, 383–6.CrossRefGoogle Scholar
  108. SATO, M., YE, L.-H. & KOHAMA, K. (1995) Myosin light chain kinase from vascular smooth muscle inhibits the ATP-dependent interaction between actin and myosin by binding to actin. J. Biochem. 118, 1–3.PubMedGoogle Scholar
  109. SELLERS, J. R. (1985) Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin. J. Biol. Chem. 260, 15815–19.PubMedGoogle Scholar
  110. SELLERS, J. R. & ADELSTEIN, R. S. (1987) Regulation of contractile activity. In The Enzymes (edited by BOYER, P. D. & KREBS, E. G.) pp. 381–418. Orlando: Academic Press.Google Scholar
  111. SELLERS, J. R. & HARVEY, E. V. (1984) Purification of myosin light chain kinase from Limulusmuscle. Biochemistry 23, 5821–6.PubMedCrossRefGoogle Scholar
  112. SELLERS, J. R. & PATO, M. D. (1984) The binding of smooth muscle myosin light chain kinase and phosphatases to actin and myosin. J. Biol. Chem. 259, 7740–6.PubMedGoogle Scholar
  113. SHIMIZU, H., ITO, M., MIYAHARA, M., ICHIKAWA, K., OKUBO, S., KONISHI, T., NAKA, M., TANAKA, T., HIRANO, K., HARTSHORNE, D. J. & NAKANO, T. (1994) Characterization of the myosin-binding subunit of smooth muscle phosphatase. J. Biol. Chem. 269, 30407–11.PubMedGoogle Scholar
  114. SHIRAZI, A., IIZUKA, K., FADDEN, P., MOSSE, C., SOMLYO, A. P., SOMLYO, A. V. & HAYSTEAD, T. A. J. (1994) Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. J. Biol. Chem. 269, 31598–606.PubMedGoogle Scholar
  115. SHIRINSKY, V. PfVOROTNIKOV, A. V., BIRUKOV, K. G., NANAEV, A. K., COLLINGE, M., LUKAS, T. J., SELLERS, J. R. & WATTERSON, D. M. (1993) A kinase-related protein stabilizes unphosphorylated smooth muscle myosin minifilaments in the presence of ATP. J. Biol. Chem. 268, 16578–83.PubMedGoogle Scholar
  116. SHOEMAKER, M. O, LAU, W., SHATTUCK, R. L., KWIATKOWSKI, A. P., MATRISIAN, P. E., GUERRA-SANTOS, L., WILSON, E., LUKAS, T. J., VAN ELDIK, L. J. & WATTERSON, D. M. (1990) Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity. J. Cell Biol. 111, 1107–25.PubMedCrossRefGoogle Scholar
  117. SHRODE, L. D., KLEIN, J. D., O'NEILL, W. C. & PUTNAM, R. W. (1995) Shrinkage-induced activation of Na./H. exchange in primary rat astrocytes: role of myosin light-chain kinase. Am. J. Physiol. 209, C257–66.Google Scholar
  118. SINGER, H. A. (1990) Protein kinase C activation and myosin light chain phosphorylation in 32P-labeled arterial smooth muscle. Am. J. Physiol. 259, C631–9.Google Scholar
  119. SOBIESZEK, A. (1991) Regulation of smooth-muscle myosin-light-chain kinase. Eur. J. Biochem. 199, 735–43.Google Scholar
  120. SOBIESZEK, A., STROBL, A., ORTNER, B. & BABIYCHUK, E. B. (1993) Ca2+-calmodulin-dependent modification of smooth-muscle myosin light-chain kinase leading to its co-operative activation by calmodulin. Biochem. J. 295, 405–11.PubMedGoogle Scholar
  121. SOMLYO, A. P. & SOMLYO, A. V. (1994) Signal transduction and regulation in smooth muscle. Nature 372, 231–6.PubMedCrossRefGoogle Scholar
  122. STULL, J. T., NUNNALLY, M. H., MOORE, R. L. & BLUMENTHAL, D. K. (1985) Myosin light chain kinases and myosin phosphorylation in skeletal muscle. Adv. Enzyme Regul. 23, 123–40.PubMedCrossRefGoogle Scholar
  123. STULL, J. T., NUNNALLY, M. H., & MICHNOFF, C. H. (1986) Calmodulin-dependent protein kinases. In The Enzymes (edited by KREBS, E. G. & BOYER, P. D.) pp. 113–66. Orlando: Academic Press.Google Scholar
  124. STULL, J. T., HSU, L.-C., TANSEY, M. G. & KAMM, K. E. (1990) Myosin light chain kinase phosphorylation in tracheal smooth muscle. J. Biol. Chem. 265, 16683–90.PubMedGoogle Scholar
  125. STULL, J. T., KRUEGER, J. K., KAMM, K. E., GAO, Z.-H., ZHI, G. & PADRE, R. (1996) Myosin light chain kinase. In Biochemistry of Smooth Muscle Contraction (edited by BARANY, M.) pp. 119–30. Orlando: Academic Press.Google Scholar
  126. SU, Z., FAN, D. & GEORGE, S. E. (1994) Role of domain 3 of calmodulin in activation of calmodulin-stimulated phosphodiesterase and smooth muscle myosin light chain kinase. J. Biol. Chem. 269, 16761–5.PubMedGoogle Scholar
  127. SWEENEY, H. L., BOWMAN, B. F., & STULL, J. T. (1993) Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function. Am. J. Physiol. 264, C1085–95.Google Scholar
  128. TAN, J. L. & SPUDICH, J. A. (1990) Dictyosteliummyosin light chain kinase. Purification and characterization. J. Biol. Chem. 265, 13818–24.PubMedGoogle Scholar
  129. TAN, J. L. & SPUDICH, J. A. (1991) Characterization and bacterial expression of the Dictyosteliummuscle light chain kinase cDNA. J. Biol. Chem. 266, 16044–9.PubMedGoogle Scholar
  130. TANAKA, M., IKEBE, R., MATSUURA, M. & IKEBE, M. (1995) Pseudosubstrate sequence may not be critical for autoinhibition of smooth muscle myosin light chain kinase. EMBO J. 14, 2839–46.PubMedGoogle Scholar
  131. TANG, D.-C., STULL, J. T., KUBOTA, Y. & KAMM, K. E. (1992) Regulation of the Ca2+ dependence of smooth muscle contraction. J. Biol. Chem. 267, 11839–45.PubMedGoogle Scholar
  132. TANSEY, M. G., WORD, R. A., HIDAKA, H., SINGER, H. A., SCHWORER, C. M., KAMM, K. E. & STULL, J. T. (1992) Phosphorylation of myosin light chain kinase by the multifunctional calmodulin-dependent protein kinase II in smooth muscle cells. J. Biol. Chem. 267, 12511–16.PubMedGoogle Scholar
  133. TANSEY, M. G., LUBY-PHELPS, K., KAMM, K. E., 268, H1–10.Google Scholar
  134. WATTERSON, D. M., COLLINGE, M., LUKAS, T. J., VAN ELDIK, L. J., BIRUKOV, K. G., STEPANOVA, O. V. & SHIRINSKY, V. P. (1995) Multiple gene products are produced from a novel protein kinase transcription region. FEBS Letts 373, 217–20.CrossRefGoogle Scholar
  135. WORD, R. A., TANG, D.-C. & KAMM, K. E. (1994) Activation properties of myosin light chain kinase during contraction/relaxation cycles of tonic and phasic smooth muscles. J. Biol. Chem. 269, 21596–602.PubMedGoogle Scholar
  136. YANO, K., ARAKI, Y., HALES, S. J., TANAKA, M. & IKEBE, M. (1993) Boundary of the autoinhibitory region of smooth muscle myosin light-chain kinase. Biochemistry 32, 12054–61.PubMedCrossRefGoogle Scholar
  137. ZHI, G., HERRING, B. P. & STULL, J. T. (1994) Structural requirements for phosphorylation of myosin regulatory light chain from smooth muscle. J. Biol. Chem. 269, 24723–7.PubMedGoogle Scholar
  138. ZIMMERMAN, U. J. & SCHLAEPFER, W. W. (1995) Characterization of calcium-activated neutral protease (CANP)-associated protein kinase from bovine brain and its phosphorylation of neurofilaments. Biochem. Biophys. Res. Commun. 129, 804–11.CrossRefGoogle Scholar

Copyright information

© Chapman and Hall 1997

Authors and Affiliations

  • PATRICIA J. GALLAGHER
    • 1
  • B. PAUL HERRING
    • 1
  • JAMES T. STULL
    • 2
  1. 1.Department of Physiology and BiophysicsIndiana University School of MedicineIndianaUSA
  2. 2.Department of PhysiologyUniversity of Texas Southwestern Medical CenterDallasUSA

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