This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
5. References
Berg, J. S., Powell, B. C, and Cheney, R. E. (2001) A millennial myosin census, Mol. Biol. Cell 12, 780–794.
Cheney, R.E., O’Shea, M.K., Heuser, J.E., Coelho, M.V., Wolenski, J.S., Espreafico, E.M., Forscher, P., Larson, RE., and Mooseker, M.S. (1993) Brain myosin-V is a two-headed unconventional myosin with motor activity, Cell, 75, 13–23.
Coy, D. L., Hancock, W. O., Wagenbach, M., and Howard, J. (1999) Kinesin’s tail domain is an inhibitory regulator of the motor domain, Nat. Cell Biol. 1, 288–292.
Craig, R., Smith, R., and Kendrick-Jones, J. (1983) Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules, Nature, 302, 436–439.
Ebashi, S., and Ebashi, F. (1964) A NEW PROTEIN COPONENT PARTICIPATING IN THE SUPERPRECIPITATION OF MYOSIN B, J. Biochem., 55, 604–613.
Ebashi, S., and Ebashi, F. (1964) A NEW PROTEIN FACTOR PROMOTING CONTRACTION OF ACTOMYOSIN Nature, 203, 645–646.
Espindola, F. S., Suter, D. M., Partata, L. B., Cao, T, Wolenski, J. S., Cheney, R. E., King, S. M., and Mooseker, M. S. (2000) The light chain composition of chicken brain myosin-Va: calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN, Cell Motility & the Cytoskeleton 47, 269–281.
Gorecka, A., Aksoy, M.O., and Hartshome, D.J. (1976) The effect of phosphorylation of gizzard myosin on actin activation, Biochem. Biophys. Res. Commun., 76, 325–331.
Homma, K., Saito, J., Ikebe, R., and Ikebe, M. (2000) Ca(2+)-dependent regulation of the motor activity of myosin V, J. Biol. Chem., 275, 34766–34771.
Ikebe, M., Onishi, H., and Watanabe, S. (1977) Phosphorylation and dephosphorylation of a light chain of the chicken gizzard myosin molecule, J. Biochem., 82, 219–302.
Ikebe, M., Hinkins, S., and Hartshome, D.J. (1983) Correlation of enzymatic properties and conformation of smooth muscle myosin, Biochemistry, 22, 4580–4587.
Kendrick-Jones, J., Lehman, W., and Sent-Gyorgyi, A.G. (1970) Regulation in molluscan muscles, J. Mol. Biol., 54, 313–326.
Lymn, R.W., and Taylor, E.W. (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin, Biochemistry, 10, 4617–4624.
Mabuchi, K. (1991) Heavy-meromyosin-decorated actin filaments: a simple method to preserve actin filaments for rotary shadowing, J. Struct. Biol., 107, 22–28.
Mermall, V., Post, P. L., and Mooseker, M. S. (1998) Unconventional myosins in cell movement, membrane traffic, and signal transduction, Science 279, 527–533.
Onishi, H., and Wakabayashi, T. (1982) Electron microscopic studies of myosin molecules from chicken gizzard muscle I: the formation of the intramolecular loop in the myosin tail, J. Biochem., 92, 871–879.
Onishi, H., Wakabayashi, T., Kamata, T., and Watanabe, S. (1983) Electron microscopic studies of myosin molecules from chicken gizzard muscle II: The effect of thiophosphorylation of the 20K-dalton light chain on the ATP-induced change in the conformation of myosin monomers, J. Biochem., 94, 1147–1154.
Philo, J. S. (2000) A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions, Anal. Biochem. 279, 151–163.
Pollard, T.D., and Korn, E.D. (1971) Filaments of Amoeba proteus. II. Binding of heavy meromyosin by thin filaments in motile cytoplasmic extracts, J. Biol. Chem., 248, 4682–4690.
Reck-Peterson, S. L., Provance, D. W., Jr., Mooseker, M. S., and Mercer, J. A. (2000) Class V myosins, Biochim. Biophys. Acta 1496, 36–51.
Sellers, J. R. (2000) Myosins: a diverse superfamily, Biochim. Biophys. Acta 1496, 3–22.
Siemankowaki, R.F., Wiseman, M.O., and White, H.D. (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle, Proc. Natl. Acad. Sci. U.SA., 82, 658–662.
Slayter, H.S., and Lowey, S. (1967) Substructure of the myosin molecule as visualized by electron microscopy, Proc. Natl. Acad Sci. U.S.A., 58, 1611–1618.
Sobieszek, A. (1977) Ca-linked phosphorylation of a light chain of vertebrate smooth-muscle myosin, Eur. J. Biochem., 73, 477–483.
Stafford, W. F., 3rd (1992) Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile, Anal. Biochem., 203, 295–301.
Stein, L.A., Chock, P.B., and Eisenberg, E. (1981) Mechanism of the actomyosin ATPase: effect of actin on the ATP hydrolysis step, Proc. Natl. Acad. Sci. U.S.A., 78, 1346–1350.
Stock, M. F., Guerrero, J., Cobb, B., Eggers, C. T., Huang, T. G., Li, X., and Hackney, D. D. (1999) Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity, J. Biol. Chem., 274, 14617–14623.
Suzuki, H., Onishi, H., Takahashi, K., and Watanabe, S. (1978) Structure and function of chicken gizzard myosin, J. Biochem., 84, 1529–1542.
Tonomura, Y., Kitagawa, S., and Yoshimura, J. (1962) The initial phase of myosin A-adenosinetriphosphatase and the possible phosphorylation of myosin A, J. Biol. Chem., 237, 3660–3666.
Trybus, K.M., Huiatt, T.W., and Lowey, S. (1982) A bent monomeric conformation of myosin from smooth muscle, Pro.Natl.Acad. Sci. USA., 79, 6151–6155.
Trybus, K.M., and Lowey, S. (1984) Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength, J. Biol. Chem., 259, 8564–8571.
Trybus, K.M., Krementsova, E., Freyzon, Y. (1999) Kinetic characterization of a monomeric unconventional myosin V construct, J. Biol. Chem., 274, 27448–27456.
Verhey, K. J., and Rapoport, T. A. (2001) Kinesin carries the signal, Trends in Biochemical Sciences 26, 545–550.
Xie, X., Harrison, D.N., Schlichiting, J., Sweet, R.M., Kalabokis, V.N., Szent-Gyorgyi, A.G., and Cohen, C. (1994) Structure of the regulatory domain of scallop myosin at 2.8 A resolution, Nature, 368, 306–312.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2005 Springer Science+Business Media, Inc.
About this paper
Cite this paper
Ikebe, M., Li, Xd., Mabuchi, K., Ikebe, R. (2005). Conformational Change and Regulation of Myosin Molecules. In: Sugi, H. (eds) Sliding Filament Mechanism in Muscle Contraction. Advances in Experimental Medicine and Biology, vol 565. Springer, Boston, MA. https://doi.org/10.1007/0-387-24990-7_6
Download citation
DOI: https://doi.org/10.1007/0-387-24990-7_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-24989-6
Online ISBN: 978-0-387-24990-2
eBook Packages: MedicineMedicine (R0)