메뉴 건너뛰기




Volumn 315, Issue 3, 2004, Pages 538-545

Ca2+-induced activation of ATPase activity of myosin Va is accompanied with a large conformational change

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; CALCIUM ION; EGTAZIC ACID; MYOSIN V; RECOMBINANT PROTEIN; CALCIUM; CALMODULIN; MYO5A PROTEIN, MOUSE; MYOSIN HEAVY CHAIN; PEPTIDE FRAGMENT; POTASSIUM CHLORIDE;

EID: 1242317813     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.01.084     Document Type: Article
Times cited : (92)

References (32)
  • 2
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V., Post P.L., Mooseker M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:1998;527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 3
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: A diverse superfamily
    • Sellers J.R. Myosins: a diverse superfamily. Biochim. Biophys. Acta. 1496:2000;3-22.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 5
    • 0024251542 scopus 로고
    • A novel 190 kDa calmodulin-binding protein associated with brain actomyosin
    • Larson R.E., Pitta D.E., Ferro J.A. A novel 190. kDa calmodulin-binding protein associated with brain actomyosin Braz. J. Med. Biol. Res. 21:1988;213-217.
    • (1988) Braz. J. Med. Biol. Res. , vol.21 , pp. 213-217
    • Larson, R.E.1    Pitta, D.E.2    Ferro, J.A.3
  • 6
    • 0025276537 scopus 로고
    • Calmodulin-binding proteins and calcium/calmodulin-regulated enzyme activities associated with brain actomyosin
    • Larson R.E., Espindola F.S., Espreafico E.M. Calmodulin-binding proteins and calcium/calmodulin-regulated enzyme activities associated with brain actomyosin. J. Neurochem. 54:1990;1288-1294.
    • (1990) J. Neurochem. , vol.54 , pp. 1288-1294
    • Larson, R.E.1    Espindola, F.S.2    Espreafico, E.M.3
  • 7
    • 0026642525 scopus 로고
    • Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: A novel calmodulin-binding myosin
    • Espindola F.S., Espreafico E.M., Coelho M.V., Martins A.R., Costa F.R., Mooseker M.S., Larson R.E. Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. J. Cell Biol. 118:1992;359-368.
    • (1992) J. Cell Biol. , vol.118 , pp. 359-368
    • Espindola, F.S.1    Espreafico, E.M.2    Coelho, M.V.3    Martins, A.R.4    Costa, F.R.5    Mooseker, M.S.6    Larson, R.E.7
  • 10
    • 0034602399 scopus 로고    scopus 로고
    • Ca(2+)-dependent regulation of the motor activity of myosin V
    • Homma K., Saito J., Ikebe R., Ikebe M. Ca(2+)-dependent regulation of the motor activity of myosin V. J. Biol. Chem. 275:2000;34766-34771.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34766-34771
    • Homma, K.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 11
    • 0033600904 scopus 로고    scopus 로고
    • Kinetic characterization of a monomeric unconventional myosin V construct
    • Trybus K.M., Krementsova E., Freyzon Y. Kinetic characterization of a monomeric unconventional myosin V construct. J. Biol. Chem. 274:1999;27448- 27456.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27448-27456
    • Trybus, K.M.1    Krementsova, E.2    Freyzon, Y.3
  • 13
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 14
    • 0021351457 scopus 로고
    • Isolation and characterization of calmodulin genes from Xenopus laevis
    • Chien Y.H., Dawid I.B. Isolation and characterization of calmodulin genes from Xenopus laevis. Mol. Cell. Biol. 4:1984;507-513.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 507-513
    • Chien, Y.H.1    Dawid, I.B.2
  • 15
    • 0032528833 scopus 로고    scopus 로고
    • Characterization of the interaction of myosin with ATP analogues having the syn conformation with respect to the adenine-ribose bond
    • Maruta S., Ohki T., Kambara T., Ikebe M. Characterization of the interaction of myosin with ATP analogues having the syn conformation with respect to the adenine-ribose bond. Eur. J. Biochem. 256:1998;229-237.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 229-237
    • Maruta, S.1    Ohki, T.2    Kambara, T.3    Ikebe, M.4
  • 16
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford 3rd W.F. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203:1992;295-301.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford III, W.F.1
  • 17
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo J.S. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279:2000;151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 18
    • 0025251847 scopus 로고
    • Melting of myosin and tropomyosin: Electron microscopic observations
    • Mabuchi K. Melting of myosin and tropomyosin: electron microscopic observations. J. Struct. Biol. 103:1990;249-256.
    • (1990) J. Struct. Biol. , vol.103 , pp. 249-256
    • Mabuchi, K.1
  • 19
    • 0025990355 scopus 로고
    • Heavy-meromyosin-decorated actin filaments: A simple method to preserve actin filaments for rotary shadowing
    • Mabuchi K. Heavy-meromyosin-decorated actin filaments: a simple method to preserve actin filaments for rotary shadowing. J. Struct. Biol. 107:1991;22-28.
    • (1991) J. Struct. Biol. , vol.107 , pp. 22-28
    • Mabuchi, K.1
  • 21
  • 22
    • 0020181786 scopus 로고
    • Electron microscopic studies of myosin molecules from chicken gizzard muscle I: The formation of the intramolecular loop in the myosin tail
    • Onishi H., Wakabayashi T. Electron microscopic studies of myosin molecules from chicken gizzard muscle I: the formation of the intramolecular loop in the myosin tail. J. Biochem. 92:1982;871-879.
    • (1982) J. Biochem. , vol.92 , pp. 871-879
    • Onishi, H.1    Wakabayashi, T.2
  • 23
    • 0020678721 scopus 로고
    • Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules
    • Craig R., Smith R., Kendrick-Jones J. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature. 302:1983;436-439.
    • (1983) Nature , vol.302 , pp. 436-439
    • Craig, R.1    Smith, R.2    Kendrick-Jones, J.3
  • 24
    • 0020592181 scopus 로고
    • Correlation of enzymatic properties and conformation of smooth muscle myosin
    • Ikebe M., Hinkins S., Hartshorne D.J. Correlation of enzymatic properties and conformation of smooth muscle myosin. Biochemistry. 22:1983;4580-4587.
    • (1983) Biochemistry , vol.22 , pp. 4580-4587
    • Ikebe, M.1    Hinkins, S.2    Hartshorne, D.J.3
  • 25
    • 0020451509 scopus 로고
    • A bent monomeric conformation of myosin from smooth muscle
    • Trybus K.M., Huiatt T.W., Lowey S. A bent monomeric conformation of myosin from smooth muscle. Proc. Natl. Acad. Sci. USA. 79:1982;6151-6155.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6151-6155
    • Trybus, K.M.1    Huiatt, T.W.2    Lowey, S.3
  • 26
    • 0021084640 scopus 로고
    • Electron microscopic studies of myosin molecules from chicken gizzard muscle II: The effect of thiophosphorylation of the 20 k-dalton light chain on the ATP-induced change in the conformation of myosin monomers
    • Onishi H., Wakabayashi T., Kamata T., Watanabe S. Electron microscopic studies of myosin molecules from chicken gizzard muscle II: the effect of thiophosphorylation of the 20. k-dalton light chain on the ATP-induced change in the conformation of myosin monomers J. Biochem. 94:1983;1147-1154.
    • (1983) J. Biochem. , vol.94 , pp. 1147-1154
    • Onishi, H.1    Wakabayashi, T.2    Kamata, T.3    Watanabe, S.4
  • 28
    • 0033591331 scopus 로고    scopus 로고
    • Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity
    • Stock M.F., Guerrero J., Cobb B., Eggers C.T., Huang T.G., Li X., Hackney D.D. Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity. J. Biol. Chem. 274:1999;14617-14623.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14617-14623
    • Stock, M.F.1    Guerrero, J.2    Cobb, B.3    Eggers, C.T.4    Huang, T.G.5    Li, X.6    Hackney, D.D.7
  • 29
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motor domain [comment]
    • Coy D.L., Hancock W.O., Wagenbach M., Howard J. Kinesin's tail domain is an inhibitory regulator of the motor domain [comment]. Nat. Cell Biol. 1:1999;288-292.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 31
    • 0034616649 scopus 로고    scopus 로고
    • Direct observation of processive movement by individual myosin V molecules
    • Sakamoto T., Amitani I., Yokota E., Ando T. Direct observation of processive movement by individual myosin V molecules. Biochem. Biophys. Res. Commun. 272:2000;586-590.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 586-590
    • Sakamoto, T.1    Amitani, I.2    Yokota, E.3    Ando, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.