메뉴 건너뛰기




Volumn 373, Issue 3, 2007, Pages 587-598

The Regulation of Myosin Binding to Actin Filaments by Lethocerus Troponin

Author keywords

calcium; stretch activation; thin filament; tropomyosin; troponin C isoforms

Indexed keywords

CALCIUM; INSECT PROTEIN; MYOSIN; REGULATOR PROTEIN; TROPOMYOSIN; TROPONIN; TROPONIN C;

EID: 34748913564     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.07.066     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0018260965 scopus 로고
    • Stretch activation of muscle: function and mechanism
    • Pringle J. Stretch activation of muscle: function and mechanism. Proc. Roy. Soc. ser. B 201 (1978) 107-130
    • (1978) Proc. Roy. Soc. ser. B , vol.201 , pp. 107-130
    • Pringle, J.1
  • 5
    • 0021959902 scopus 로고
    • The effect of MgATP on forming and breaking actin-myosin linkages in contracted skinned insect flight muscle fibres
    • Kuhn H.J., Bletz C., Guth K., and Ruegg J.C. The effect of MgATP on forming and breaking actin-myosin linkages in contracted skinned insect flight muscle fibres. J. Mus. Res. Cell Motil. 6 (1985) 5-27
    • (1985) J. Mus. Res. Cell Motil. , vol.6 , pp. 5-27
    • Kuhn, H.J.1    Bletz, C.2    Guth, K.3    Ruegg, J.C.4
  • 7
    • 1842562372 scopus 로고    scopus 로고
    • A troponin switch that regulates muscle contraction by stretch instead of calcium
    • Agianian B., Krzic U., Qiu F., Linke W.A., Leonard K., and Bullard B. A troponin switch that regulates muscle contraction by stretch instead of calcium. EMBO J. 23 (2004) 772-779
    • (2004) EMBO J. , vol.23 , pp. 772-779
    • Agianian, B.1    Krzic, U.2    Qiu, F.3    Linke, W.A.4    Leonard, K.5    Bullard, B.6
  • 10
    • 0037570580 scopus 로고    scopus 로고
    • Troponin C in different insect muscle types: identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect
    • Qiu F., Lakey A., Agianian B., Hutchings A., Butcher G.W., Labeit S., et al. Troponin C in different insect muscle types: identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect. Biochem. J. 371 (2003) 811-821
    • (2003) Biochem. J. , vol.371 , pp. 811-821
    • Qiu, F.1    Lakey, A.2    Agianian, B.3    Hutchings, A.4    Butcher, G.W.5    Labeit, S.6
  • 11
    • 18244430240 scopus 로고    scopus 로고
    • Structure of the Lethocerus troponin-tropomyosin complex as determined by electron microscopy
    • Wendt T., Guenebaut V., and Leonard K.R. Structure of the Lethocerus troponin-tropomyosin complex as determined by electron microscopy. J. Struct. Biol. 118 (1997) 1-8
    • (1997) J. Struct. Biol. , vol.118 , pp. 1-8
    • Wendt, T.1    Guenebaut, V.2    Leonard, K.R.3
  • 12
    • 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., and 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
  • 13
    • 0022381827 scopus 로고
    • The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin
    • Criddle A.H., Geeves M.A., and Jeffries T. The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem. J. 232 (1985) 343-349
    • (1985) Biochem. J. , vol.232 , pp. 343-349
    • Criddle, A.H.1    Geeves, M.A.2    Jeffries, T.3
  • 14
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds A.G., and Taylor R.S. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 257 (1975) 54-56
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 16
    • 0023640537 scopus 로고
    • The effect of temperature and ionic strength on the apparent Ca-affinity of EGTA and the analogous Ca-chelators BAPTA and dibromo-BAPTA
    • Harrison S.M., and Bers D.M. The effect of temperature and ionic strength on the apparent Ca-affinity of EGTA and the analogous Ca-chelators BAPTA and dibromo-BAPTA. Biochim. Biophys. Acta 925 (1987) 133-143
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 133-143
    • Harrison, S.M.1    Bers, D.M.2
  • 17
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop D.F., and Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65 (1993) 693-701
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 18
    • 0034703378 scopus 로고    scopus 로고
    • Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
    • Lehman W., Hatch V., Korman V., Rosol M., Thomas L., Maytum R., et al. Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments. J. Mol. Biol. 302 (2000) 593-606
    • (2000) J. Mol. Biol. , vol.302 , pp. 593-606
    • Lehman, W.1    Hatch, V.2    Korman, V.3    Rosol, M.4    Thomas, L.5    Maytum, R.6
  • 19
    • 0028887715 scopus 로고
    • Characterization of the equilibrium between blocked and closed states of muscle thin filaments
    • Head J.G., Ritchie M.D., and Geeves M.A. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur. J. Biochem. 227 (1995) 694-699
    • (1995) Eur. J. Biochem. , vol.227 , pp. 694-699
    • Head, J.G.1    Ritchie, M.D.2    Geeves, M.A.3
  • 20
    • 0019128230 scopus 로고
    • Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
    • Trybus K.M., and Taylor E.W. Kinetic studies of the cooperative binding of subfragment 1 to regulated actin. Proc. Natl Acad. Sci. USA 77 (1980) 7209-7213
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7209-7213
    • Trybus, K.M.1    Taylor, E.W.2
  • 21
    • 4444281053 scopus 로고    scopus 로고
    • 2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications
    • 2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications. Biophys. J. 87 (2004) 1825-1835
    • (2004) Biophys. J. , vol.87 , pp. 1825-1835
    • Gafurov, B.1    Chen, Y.D.2    Chalovich, J.M.3
  • 22
    • 0035042523 scopus 로고    scopus 로고
    • Theoretical kinetic studies of models for binding myosin subfragment-1 to regulated actin: Hill model versus Geeves model
    • Chen Y., Yan B., Chalovich J.M., and Brenner B. Theoretical kinetic studies of models for binding myosin subfragment-1 to regulated actin: Hill model versus Geeves model. Biophys. J. 80 (2001) 2338-2349
    • (2001) Biophys. J. , vol.80 , pp. 2338-2349
    • Chen, Y.1    Yan, B.2    Chalovich, J.M.3    Brenner, B.4
  • 23
    • 0033619726 scopus 로고    scopus 로고
    • The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state
    • Moraczewska J., Nicholson-Flynn K., and Hitchcock-DeGregori S.E. The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state. Biochemistry 38 (1999) 15885-15892
    • (1999) Biochemistry , vol.38 , pp. 15885-15892
    • Moraczewska, J.1    Nicholson-Flynn, K.2    Hitchcock-DeGregori, S.E.3
  • 24
    • 0033615687 scopus 로고    scopus 로고
    • Effects of tropomyosin internal deletions on thin filament function
    • Landis C., Back N., Homsher E., and Tobacman L.S. Effects of tropomyosin internal deletions on thin filament function. J. Biol. Chem. 274 (1999) 31279-31285
    • (1999) J. Biol. Chem. , vol.274 , pp. 31279-31285
    • Landis, C.1    Back, N.2    Homsher, E.3    Tobacman, L.S.4
  • 25
    • 0037470225 scopus 로고    scopus 로고
    • Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms
    • Maytum R., Westerdorf B., Jaquet K., and Geeves M.A. Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms. J. Biol. Chem. 278 (2003) 6696-6701
    • (2003) J. Biol. Chem. , vol.278 , pp. 6696-6701
    • Maytum, R.1    Westerdorf, B.2    Jaquet, K.3    Geeves, M.A.4
  • 26
    • 33645231253 scopus 로고    scopus 로고
    • Role of calcium in the regulation of mechanical power in insect flight
    • Gordon S., and Dickinson M.H. Role of calcium in the regulation of mechanical power in insect flight. Proc. Natl Acad. Sci. USA 103 (2006) 4311-4315
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4311-4315
    • Gordon, S.1    Dickinson, M.H.2
  • 27
    • 0018328198 scopus 로고
    • Structure of the backbone in myosin filaments of muscle
    • Wray J.S. Structure of the backbone in myosin filaments of muscle. Nature 277 (1979) 37-40
    • (1979) Nature , vol.277 , pp. 37-40
    • Wray, J.S.1
  • 28
    • 0013407336 scopus 로고
    • Mechanics and protein content of insect flight muscle
    • Peckham M., Cripps R., White D., and Bullard B. Mechanics and protein content of insect flight muscle. J. Exp. Biol. 168 (1992) 57-76
    • (1992) J. Exp. Biol. , vol.168 , pp. 57-76
    • Peckham, M.1    Cripps, R.2    White, D.3    Bullard, B.4
  • 30
    • 33745686007 scopus 로고    scopus 로고
    • The structural role of high molecular weight tropomyosins in dipteran indirect flight muscle and the effect of phosphorylation
    • Mateos J., Herranz R., Domingo A., Sparrow J., and Marco R. The structural role of high molecular weight tropomyosins in dipteran indirect flight muscle and the effect of phosphorylation. J. Mus. Res. Cell Motil. 27 (2006) 189-201
    • (2006) J. Mus. Res. Cell Motil. , vol.27 , pp. 189-201
    • Mateos, J.1    Herranz, R.2    Domingo, A.3    Sparrow, J.4    Marco, R.5
  • 31
    • 1542315447 scopus 로고    scopus 로고
    • Drosophila muscle regulation characterized by electron microscopy and three-dimensional reconstruction of thin filament mutants
    • Cammarato A., Hatch V., Saide J., Craig R., Sparrow J.C., Tobacman L.S., and Lehman W. Drosophila muscle regulation characterized by electron microscopy and three-dimensional reconstruction of thin filament mutants. Biophys. J. 86 (2004) 1618-1624
    • (2004) Biophys. J. , vol.86 , pp. 1618-1624
    • Cammarato, A.1    Hatch, V.2    Saide, J.3    Craig, R.4    Sparrow, J.C.5    Tobacman, L.S.6    Lehman, W.7
  • 34
    • 24644523695 scopus 로고    scopus 로고
    • Comparative studies on the functional roles of N- and C-terminal regions of molluskan and vertebrate troponin-I
    • Tanaka H., Takeya Y., Doi T., Yumoto F., Tanokura M., Ohtsuki I., et al. Comparative studies on the functional roles of N- and C-terminal regions of molluskan and vertebrate troponin-I. FEBS J. 272 (2005) 4475-4486
    • (2005) FEBS J. , vol.272 , pp. 4475-4486
    • Tanaka, H.1    Takeya, Y.2    Doi, T.3    Yumoto, F.4    Tanokura, M.5    Ohtsuki, I.6
  • 35
    • 0346118918 scopus 로고    scopus 로고
    • Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling
    • Miller B.M., Nyitrai M., Bernstein S.I., and Geeves M.A. Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling. J. Biol. Chem. 278 (2003) 50293-50300
    • (2003) J. Biol. Chem. , vol.278 , pp. 50293-50300
    • Miller, B.M.1    Nyitrai, M.2    Bernstein, S.I.3    Geeves, M.A.4
  • 36
    • 0942268804 scopus 로고    scopus 로고
    • Isolation and kinetic characterisation of myosin and myosin S1 from the Drosophila indirect flight muscles
    • Silva R., Sparrow J.C., and Geeves M.A. Isolation and kinetic characterisation of myosin and myosin S1 from the Drosophila indirect flight muscles. J. Mus. Res. Cell Motil. 24 (2003) 489-498
    • (2003) J. Mus. Res. Cell Motil. , vol.24 , pp. 489-498
    • Silva, R.1    Sparrow, J.C.2    Geeves, M.A.3
  • 37
    • 0015791929 scopus 로고
    • The contractile and regulatory proteins of insect flight muscle
    • Bullard B., Dabrowska R., and Winkelman L. The contractile and regulatory proteins of insect flight muscle. Biochem. J. 135 (1973) 277-286
    • (1973) Biochem. J. , vol.135 , pp. 277-286
    • Bullard, B.1    Dabrowska, R.2    Winkelman, L.3
  • 38
    • 0023548409 scopus 로고
    • Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements
    • White D.C., Ricigliano J.W., and Webb M.R. Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements. J. Mus. Res. Cell Motil. 8 (1987) 537-540
    • (1987) J. Mus. Res. Cell Motil. , vol.8 , pp. 537-540
    • White, D.C.1    Ricigliano, J.W.2    Webb, M.R.3
  • 39
    • 0022704128 scopus 로고
    • The ATPase kinetics of insect fibrillar flight muscle myosin subfragment-1
    • White D.C., Zimmerman R.W., and Trentham D.R. The ATPase kinetics of insect fibrillar flight muscle myosin subfragment-1. J. Mus. Res. Cell Motil. 7 (1986) 179-192
    • (1986) J. Mus. Res. Cell Motil. , vol.7 , pp. 179-192
    • White, D.C.1    Zimmerman, R.W.2    Trentham, D.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.