메뉴 건너뛰기




Volumn 1700, Issue 2, 2004, Pages 171-178

Evidence for a direct but sequential binding of titin to tropomyosin and actin filaments

Author keywords

Interaction; Thin filament; Titin; Tropomyosin

Indexed keywords

ACTIN; CONNECTIN; MYOSIN; TROPOMYOSIN;

EID: 3242741080     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.05.001     Document Type: Article
Times cited : (20)

References (49)
  • 1
    • 0037569632 scopus 로고    scopus 로고
    • Unfolding of titin domains studied by molecular dynamics simulations
    • Gao M., Lu H., Schulten K. Unfolding of titin domains studied by molecular dynamics simulations. J. Muscle Res. Cell Motil. 23:2002;513-521
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , pp. 513-521
    • Gao, M.1    Lu, H.2    Schulten, K.3
  • 5
    • 0036947533 scopus 로고    scopus 로고
    • Titin: An endosarcomeric protein that modulates myocardial stiffness in DCM
    • Wu Y., Labeit S., Lewinter M.M., Granzier H. Titin: an endosarcomeric protein that modulates myocardial stiffness in DCM. J. Card. Fail. 8:2002;S276-S286
    • (2002) J. Card. Fail. , vol.8 , pp. 276-S286
    • Wu, Y.1    Labeit, S.2    Lewinter, M.M.3    Granzier, H.4
  • 9
    • 0031172869 scopus 로고    scopus 로고
    • Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs
    • Kinbara K., Sorimachi H., Ishiura S., Suzuki K. Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs. Arch. Biochem. Biophys. 342:1997;99-107
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 99-107
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 10
    • 0034472156 scopus 로고    scopus 로고
    • Probing the functional roles of titin ligands in cardiac myofibril assembly and maintenance
    • (discussion 86-8)
    • McElhinny A.S., Labeit S., Gregorio C.C. Probing the functional roles of titin ligands in cardiac myofibril assembly and maintenance. Adv. Exp. Med. Biol. 481:2000;67-86. (discussion 86-8)
    • (2000) Adv. Exp. Med. Biol. , vol.481 , pp. 67-86
    • McElhinny, A.S.1    Labeit, S.2    Gregorio, C.C.3
  • 11
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang M.L., Centner T., Fornoff F., Geach A.J., Gotthardt M., McNabb M., Witt C.C., Labeit D., Gregorio C.C., Granzier H., Labeit S. The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ. Res. 89:2001;1065-1072
    • (2001) Circ. Res. , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5    McNabb, M.6    Witt, C.C.7    Labeit, D.8    Gregorio, C.C.9    Granzier, H.10    Labeit, S.11
  • 13
    • 0030976481 scopus 로고    scopus 로고
    • Interaction between titin and thin filaments in intact cardiac muscle
    • Trombitas K., Greaser M.L., Pollack G.H. Interaction between titin and thin filaments in intact cardiac muscle. J. Muscle Res. Cell Motil. 18:1997;345-351
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 345-351
    • Trombitas, K.1    Greaser, M.L.2    Pollack, G.H.3
  • 16
    • 0020023850 scopus 로고
    • Preparation and identification of alpha- and beta-tropomyosins
    • Smillie L.B. Preparation and identification of alpha- and beta-tropomyosins. Methods Enzymol. 85(Pt B):1982;234-241
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 234-241
    • Smillie, L.B.1
  • 17
    • 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
  • 18
    • 0025603713 scopus 로고
    • Localization of a new alpha-actinin binding site in the COOH-terminal part of actin sequence
    • Lebart M.C., Mejean C., Boyer M., Roustan C., Benyamin Y. Localization of a new alpha-actinin binding site in the COOH-terminal part of actin sequence. Biochem. Biophys. Res. Commun. 173:1990;120-126
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 120-126
    • Lebart, M.C.1    Mejean, C.2    Boyer, M.3    Roustan, C.4    Benyamin, Y.5
  • 19
    • 0027419031 scopus 로고
    • Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide
    • Astier C., Labbe J.P., Roustan C., Benyamin Y. Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide. Biochem. J. 290(Pt 3):1993;731-734
    • (1993) Biochem. J. , vol.290 , Issue.PART 3 , pp. 731-734
    • Astier, C.1    Labbe, J.P.2    Roustan, C.3    Benyamin, Y.4
  • 21
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
    • Furst D.O., Osborn M., Nave R., Weber K. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J. Cell Biol. 106:1988;1563-1572
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Furst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 22
    • 0029143271 scopus 로고
    • Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases
    • Sebestyen M.G., Wolff J.A., Greaser M.L. Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases. J. Cell. Sci. 108:1995;3029-3037
    • (1995) J. Cell. Sci. , vol.108 , pp. 3029-3037
    • Sebestyen, M.G.1    Wolff, J.A.2    Greaser, M.L.3
  • 23
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S., Kolmerer B. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:1995;293-296
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin J.C., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 20:1999;3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 0020021880 scopus 로고
    • Preparation of smooth muscle alpha-actinin
    • Craig S.W., Lancashire C.L., Cooper J.A. Preparation of smooth muscle alpha-actinin. Methods Enzymol. 1(85 Pt B):1982;316-321
    • (1982) Methods Enzymol. , vol.1 , Issue.85 PART B , pp. 316-321
    • Craig, S.W.1    Lancashire, C.L.2    Cooper, J.A.3
  • 26
    • 0022645234 scopus 로고
    • Anti-actin antibodies: Chemical modification allows the selective production of antibodies to the N-terminal region
    • Benyamin Y., Roustan C., Boyer M. Anti-actin antibodies: chemical modification allows the selective production of antibodies to the N-terminal region. J. Immunol. Methods. 86:1986;21-29
    • (1986) J. Immunol. Methods , vol.86 , pp. 21-29
    • Benyamin, Y.1    Roustan, C.2    Boyer, M.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld J., Capdevielle J., Guillemot J.-C., Ferrara P. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203:1992;173-179
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.-C.3    Ferrara, P.4
  • 31
    • 0347355504 scopus 로고    scopus 로고
    • Myofibrillar tightly bound calcium in skeletal muscle fibers: A possible role of this cation in titin strands aggregation
    • Coulis G., Sentandreu M.A., Bleimling N., Gautel M., Benyamin Y., Ouali A. Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation. FEBS Lett. 556:2004;271-275
    • (2004) FEBS Lett. , vol.556 , pp. 271-275
    • Coulis, G.1    Sentandreu, M.A.2    Bleimling, N.3    Gautel, M.4    Benyamin, Y.5    Ouali, A.6
  • 33
    • 0031691961 scopus 로고    scopus 로고
    • PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10
    • Trombitas K., Greaser M., French G., Granzier H. PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10. J. Struct. Biol. 122:1998;188-196
    • (1998) J. Struct. Biol. , vol.122 , pp. 188-196
    • Trombitas, K.1    Greaser, M.2    French, G.3    Granzier, H.4
  • 34
    • 0022079716 scopus 로고
    • Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils
    • Wang S.M., Greaser M.L. Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils. J. Muscle Res. Cell Motil. 6:1985;293-312
    • (1985) J. Muscle Res. Cell Motil. , vol.6 , pp. 293-312
    • Wang, S.M.1    Greaser, M.L.2
  • 42
    • 0035666357 scopus 로고    scopus 로고
    • Ion-dependence of Z-line and M-line response to calcium in striated muscle fibres in rigor
    • Coomber S.J., Taracewicz E., Akhtar S., deHaan A., Elliott G.F. Ion-dependence of Z-line and M-line response to calcium in striated muscle fibres in rigor. Cell Calcium. 30:2001;297-309
    • (2001) Cell Calcium , vol.30 , pp. 297-309
    • Coomber, S.J.1    Taracewicz, E.2    Akhtar, S.3    Dehaan, A.4    Elliott, G.F.5
  • 43
    • 0032026522 scopus 로고    scopus 로고
    • Ca(2+)-dependence of diastolic properties of cardiac sarcomeres: Involvement of titin
    • Stuyvers B.D., Miura M., Jin J.P., ter Keurs H.E. Ca(2+)-dependence of diastolic properties of cardiac sarcomeres: involvement of titin. Prog. Biophys. Mol. Biol. 69:1998;425-443
    • (1998) Prog. Biophys. Mol. Biol. , vol.69 , pp. 425-443
    • Stuyvers, B.D.1    Miura, M.2    Jin, J.P.3    Ter Keurs, H.E.4
  • 45
    • 0034470438 scopus 로고    scopus 로고
    • Is titin the length sensor in cardiac muscle? Physiological and physiopathological perspectives
    • (discussion 348-351)
    • Le Guennec J.Y., Cazorla O., Lacampagne A., Vassort G. Is titin the length sensor in cardiac muscle? Physiological and physiopathological perspectives. Adv. Exp. Med. Biol. 481:2000;337-348. (discussion 348-351)
    • (2000) Adv. Exp. Med. Biol. , vol.481 , pp. 337-348
    • Le Guennec, J.Y.1    Cazorla, O.2    Lacampagne, A.3    Vassort, G.4
  • 46
    • 0033151961 scopus 로고    scopus 로고
    • Length modulation of active force in rat cardiac myocytes: Is titin the sensor?
    • Cazorla O., Vassort G., Garnier D., Le Guennec J.Y. Length modulation of active force in rat cardiac myocytes: is titin the sensor? J. Mol. Cell. Cardiol. 31:1999;1215-1227
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 1215-1227
    • Cazorla, O.1    Vassort, G.2    Garnier, D.3    Le Guennec, J.Y.4
  • 47
    • 0036370089 scopus 로고    scopus 로고
    • Divergent abnormal muscle relaxation by hypertrophic cardiomyopathy and nemaline myopathy mutant tropomyosins
    • Michele D.E., Coutu P., Metzger J.M. Divergent abnormal muscle relaxation by hypertrophic cardiomyopathy and nemaline myopathy mutant tropomyosins. Physiol. Genomics. 9:2002;103-111
    • (2002) Physiol. Genomics , vol.9 , pp. 103-111
    • Michele, D.E.1    Coutu, P.2    Metzger, J.M.3
  • 48
    • 0037047648 scopus 로고    scopus 로고
    • Cardiac dysfunction in hypertrophic cardiomyopathy mutant tropomyosin mice is transgene-dependent, hypertrophy-independent, and improved by beta-blockade
    • Michele D.E., Gomez C.A., Hong K.E., Westfall M.V., Metzger J.M. Cardiac dysfunction in hypertrophic cardiomyopathy mutant tropomyosin mice is transgene-dependent, hypertrophy-independent, and improved by beta-blockade. Circ. Res. 91:2002;255-262
    • (2002) Circ. Res. , vol.91 , pp. 255-262
    • Michele, D.E.1    Gomez, C.A.2    Hong, K.E.3    Westfall, M.V.4    Metzger, J.M.5
  • 49
    • 0042857127 scopus 로고    scopus 로고
    • Cardiomyopathy: Molecular and immunological aspects (Review)
    • Takeda N. Cardiomyopathy: molecular and immunological aspects (Review). Int. J. Mol. Med. 11:2003;13-16
    • (2003) Int. J. Mol. Med. , vol.11 , pp. 13-16
    • Takeda, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.