ORGANIZATION OF MYOSIN LIGHT CHAIN KINASE FROM RABBIT SKELETAL MUSCLE
作者： Peter J. Kennelly , Koji Takio , Donald K. Blumenthal , Arthur M. Edelman , Moira B. Glaccum
DOI: 10.1016/B978-0-12-521040-9.50091-7
关键词:
摘要: Publisher Summary This chapter elaborates the organization of myosin light chain kinase from rabbit skeletal muscle. The kinases comprise a family tissue-specific isozymes whose function is to phosphorylate one components, P- or DTNB-light chain, myosin. Distinct isozyme forms Myosin Light Chain Kinase (MLCK) have been identified in skeletal, cardiac and smooth In addition, MLCK has detected nonmuscle tisues such as brain, T-cells, platelets cultured fibroblasts. All share several properties common. are monomers sole physiological appears be phosphorylating P-light Skeletal transfers gamma phosphoryl group ATP onto serine residue located at position 15 chain. reaction requires presence Mg 2+ . viewed being very substrate specific, only that it will with high efficiency chains. It found unlike its muscle counterpart, phosphorylates not indigenous but also those muscles.
sci-hub.st 参考文章(48)
Georg W. Mayr, Ludwig M.G. Heilmeyer, Skeletal muscle myosin light chain kinase FEBS Letters. ,vol. 157, pp. 225- 231 ,(1983) , 10.1016/0014-5793(83)80552-3
G A Klug, B R Botterman, J T Stull, The effect of low frequency stimulation on myosin light chain phosphorylation in skeletal muscle. Journal of Biological Chemistry. ,vol. 257, pp. 4688- 4690 ,(1982) , 10.1016/S0021-9258(18)34577-0
James T. Stull, Donald K. Blumenthal, Roger Cooke, Regulation of contraction by myosin phosphorylation. A comparison between smooth and skeletal muscles. Biochemical Pharmacology. ,vol. 29, pp. 2537- 2543 ,(1980) , 10.1016/0006-2952(80)90063-5
M H Nunnally, S B Rybicki, J T Stull, Characterization of chicken skeletal muscle myosin light chain kinase. Evidence for muscle-specific isozymes. Journal of Biological Chemistry. ,vol. 260, pp. 1020- 1026 ,(1985) , 10.1016/S0021-9258(20)71202-0
J.D. Johnson, M.J. Holroyde, T.H. Crouch, R.J. Solaro, J.D. Potter, Fluorescence studies of the interaction of calmodulin with myosin light chain kinase. Journal of Biological Chemistry. ,vol. 256, pp. 12194- 12198 ,(1981) , 10.1016/S0021-9258(18)43252-8
M.P. Walsh, B. Vallet, J.C. Cavadore, J.G. Demaille, Homologous calcium-binding proteins in the activation of skeletal, cardiac, and smooth muscle myosin light chain kinases. Journal of Biological Chemistry. ,vol. 255, pp. 335- 337 ,(1980) , 10.1016/S0021-9258(19)86172-0
C H Michnoff, B E Kemp, J T Stull, Phosphorylation of synthetic peptides by skeletal muscle myosin light chain kinases. Journal of Biological Chemistry. ,vol. 261, pp. 8320- 8326 ,(1986) , 10.1016/S0021-9258(19)83915-7
A M Edelman, K Takio, D K Blumenthal, R S Hansen, K A Walsh, K Titani, E G Krebs, Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. Journal of Biological Chemistry. ,vol. 260, pp. 11275- 11285 ,(1985) , 10.1016/S0021-9258(17)39177-9
J L Daniel, I R Molish, M Rigmaiden, G Stewart, Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response. Journal of Biological Chemistry. ,vol. 259, pp. 9826- 9831 ,(1984) , 10.1016/S0021-9258(17)42774-8
M.P. Walsh, B. Vallet, F. Autric, J.G. Demaille, Purification and characterization of bovine cardiac calmodulin-dependent myosin light chain kinase. Journal of Biological Chemistry. ,vol. 254, pp. 12136- 12144 ,(1979) , 10.1016/S0021-9258(19)86440-2