메뉴 건너뛰기




Volumn 412, Issue 3, 2011, Pages 379-386

The N-terminal domains of myosin binding protein C can bind polymorphically to F-actin

Author keywords

electron microscopy; helical polymers; muscle contraction; three dimensional reconstruction

Indexed keywords

F ACTIN; MYOSIN BINDING PROTEIN C; TROPOMYOSIN;

EID: 80052368421     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.056     Document Type: Article
Times cited : (48)

References (46)
  • 1
    • 0029917475 scopus 로고    scopus 로고
    • A personal view of muscle and motility mechanisms
    • Huxley H.E. A personal view of muscle and motility mechanisms Annu. Rev. Physiol. 58 1996 1 19 (Pubitemid 26106711)
    • (1996) Annual Review of Physiology , vol.58 , pp. 1-19
    • Huxley, H.E.1
  • 2
    • 0015530296 scopus 로고
    • Regulation of skeletal muscle contraction: II. Structural studies of the interaction of the tropomyosin-troponin complex with actin
    • Spudich J.A., Huxley H.E., and Finch J.T. Regulation of skeletal muscle contraction: II. Structural studies of the interaction of the tropomyosin-troponin complex with actin J. Mol. Biol. 72 1972 619 632
    • (1972) J. Mol. Biol. , vol.72 , pp. 619-632
    • Spudich, J.A.1    Huxley, H.E.2    Finch, J.T.3
  • 3
    • 67349282758 scopus 로고    scopus 로고
    • Structural basis for the activation of muscle contraction by troponin and tropomyosin
    • Lehman W., Galinska-Rakoczy A., Hatch V., Tobacman L.S., and Craig R. Structural basis for the activation of muscle contraction by troponin and tropomyosin J. Mol. Biol. 388 2009 673 681
    • (2009) J. Mol. Biol. , vol.388 , pp. 673-681
    • Lehman, W.1    Galinska-Rakoczy, A.2    Hatch, V.3    Tobacman, L.S.4    Craig, R.5
  • 4
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • Lehman W., Vibert P., Uman P., and Craig R. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments J. Mol. Biol. 251 1995 191 196
    • (1995) J. Mol. Biol. , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 5
    • 77955730763 scopus 로고    scopus 로고
    • Evolution of the regulatory control of vertebrate striated muscle: The roles of troponin i and myosin binding protein-C
    • Shaffer J.F., and Gillis T.E. Evolution of the regulatory control of vertebrate striated muscle: the roles of troponin I and myosin binding protein-C Physiol. Genomics 42 2010 406 419
    • (2010) Physiol. Genomics , vol.42 , pp. 406-419
    • Shaffer, J.F.1    Gillis, T.E.2
  • 6
    • 79953184636 scopus 로고    scopus 로고
    • Signaling and myosin-binding protein C
    • James J., and Robbins J. Signaling and myosin-binding protein C J. Biol. Chem. 286 2011 9913 9919
    • (2011) J. Biol. Chem. , vol.286 , pp. 9913-9919
    • James, J.1    Robbins, J.2
  • 8
    • 0034976642 scopus 로고    scopus 로고
    • The molecular genetic basis for hypertrophic cardiomyopathy
    • DOI 10.1006/jmcc.2001.1340
    • Marian A.J., and Roberts R. The molecular genetic basis for hypertrophic cardiomyopathy J. Mol. Cell. Cardiol. 33 2001 655 670 (Pubitemid 32538979)
    • (2001) Journal of Molecular and Cellular Cardiology , vol.33 , Issue.4 , pp. 655-670
    • Marian, A.J.1    Roberts, R.2
  • 10
    • 79960996049 scopus 로고    scopus 로고
    • Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle
    • Luther P.K., Winkler H., Taylor K., Zoghbi M.E., Craig R., and Padron R. Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle Proc. Natl Acad. Sci. USA 108 2011 11423 11428
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 11423-11428
    • Luther, P.K.1    Winkler, H.2    Taylor, K.3    Zoghbi, M.E.4    Craig, R.5    Padron, R.6
  • 11
    • 77951023705 scopus 로고    scopus 로고
    • Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C
    • Shaffer J.F., and Harris S.P. Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C J. Muscle Res. Cell Motil. 30 2009 303 306
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 303-306
    • Shaffer, J.F.1    Harris, S.P.2
  • 12
    • 77951024549 scopus 로고    scopus 로고
    • Functional differences between the N-terminal domains of mouse and human myosin binding protein-C
    • Shaffer J.F., Wong P., Bezold K.L., and Harris S.P. Functional differences between the N-terminal domains of mouse and human myosin binding protein-C J. Biomed. Biotechnol. 2010 2010 789 798
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 789-798
    • Shaffer, J.F.1    Wong, P.2    Bezold, K.L.3    Harris, S.P.4
  • 13
    • 0035895938 scopus 로고    scopus 로고
    • Hypercontractile properties of cardiac muscle fibers in a knock-in mouse model of cardiac myosin-binding protein-C
    • Witt C.C., Gerull B., Davies M.J., Centner T., Linke W.A., and Thierfelder L. Hypercontractile properties of cardiac muscle fibers in a knock-in mouse model of cardiac myosin-binding protein-C J. Biol. Chem. 276 2001 5353 5359
    • (2001) J. Biol. Chem. , vol.276 , pp. 5353-5359
    • Witt, C.C.1    Gerull, B.2    Davies, M.J.3    Centner, T.4    Linke, W.A.5    Thierfelder, L.6
  • 14
    • 79952454934 scopus 로고    scopus 로고
    • Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin
    • Kensler R.W., Shaffer J.F., and Harris S.P. Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin J. Struct. Biol. 174 2011 44 51
    • (2011) J. Struct. Biol. , vol.174 , pp. 44-51
    • Kensler, R.W.1    Shaffer, J.F.2    Harris, S.P.3
  • 15
    • 57449111078 scopus 로고    scopus 로고
    • Cardiac myosin-binding protein C decorates F-actin: Implications for cardiac function
    • Whitten A.E., Jeffries C.M., Harris S.P., and Trewhella J. Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function Proc. Natl Acad. Sci. USA 105 2008 18360 18365
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 18360-18365
    • Whitten, A.E.1    Jeffries, C.M.2    Harris, S.P.3    Trewhella, J.4
  • 16
    • 40849123741 scopus 로고    scopus 로고
    • Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C
    • Jeffries C.M., Whitten A.E., Harris S.P., and Trewhella J. Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C J. Mol. Biol. 377 2008 1186 1199
    • (2008) J. Mol. Biol. , vol.377 , pp. 1186-1199
    • Jeffries, C.M.1    Whitten, A.E.2    Harris, S.P.3    Trewhella, J.4
  • 18
    • 66449110385 scopus 로고    scopus 로고
    • The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner
    • Shaffer J.F., Kensler R.W., and Harris S.P. The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner J. Biol. Chem. 284 2009 12318 12327
    • (2009) J. Biol. Chem. , vol.284 , pp. 12318-12327
    • Shaffer, J.F.1    Kensler, R.W.2    Harris, S.P.3
  • 19
    • 41249089916 scopus 로고    scopus 로고
    • Crystal structure of the C1 domain of cardiac myosin binding protein-C: Implications for hypertrophic cardiomyopathy
    • Govada L., Carpenter L., da Fonseca P.C., Helliwell J.R., Rizkallah P., and Flashman E. Crystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathy J. Mol. Biol. 378 2008 387 397
    • (2008) J. Mol. Biol. , vol.378 , pp. 387-397
    • Govada, L.1    Carpenter, L.2    Da Fonseca, P.C.3    Helliwell, J.R.4    Rizkallah, P.5    Flashman, E.6
  • 20
    • 0027328612 scopus 로고
    • A conformational change in the actin subunit can change the flexibility of the actin filament
    • DOI 10.1006/jmbi.1993.1393
    • Orlova A., and Egelman E.H. A conformational change in the actin subunit can change the flexibility of the actin filament J. Mol. Biol. 232 1993 334 341 (Pubitemid 23251162)
    • (1993) Journal of Molecular Biology , vol.232 , Issue.2 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 21
    • 48049098171 scopus 로고    scopus 로고
    • Cofilin increases the bending flexibility of actin filaments: Implications for severing and cell mechanics
    • McCullough B.R., Blanchoin L., Martiel J.L., and De La Cruz E.M. Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics J. Mol. Biol. 381 2008 550 558
    • (2008) J. Mol. Biol. , vol.381 , pp. 550-558
    • McCullough, B.R.1    Blanchoin, L.2    Martiel, J.L.3    De La Cruz, E.M.4
  • 22
    • 0346849714 scopus 로고    scopus 로고
    • ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments
    • DOI 10.1083/jcb.200308144
    • Galkin V.E., Orlova A., VanLoock M.S., Shvetsov A., Reisler E., and Egelman E.H. ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments J. Cell Biol. 163 2003 1057 1066 (Pubitemid 37541881)
    • (2003) Journal of Cell Biology , vol.163 , Issue.5 , pp. 1057-1066
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Shvetsov, A.4    Reisler, E.5    Egelman, E.H.6
  • 24
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii T., Iwane A.H., Yanagida T., and Namba K. Direct visualization of secondary structures of F-actin by electron cryomicroscopy Nature 467 2010 724 728
    • (2010) Nature , vol.467 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 25
    • 78751475039 scopus 로고    scopus 로고
    • Myosin binding protein C interaction with actin: Characterization and mapping of the binding site
    • Rybakova I.N., Greaser M.L., and Moss R.L. Myosin binding protein C interaction with actin: characterization and mapping of the binding site J. Biol. Chem. 286 2011 2008 2016
    • (2011) J. Biol. Chem. , vol.286 , pp. 2008-2016
    • Rybakova, I.N.1    Greaser, M.L.2    Moss, R.L.3
  • 26
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira P. Modular organization of actin crosslinking proteins Trends Biochem. Sci. 16 1991 87 92 (Pubitemid 121004410)
    • (1991) Trends in Biochemical Sciences , vol.16 , Issue.1 , pp. 87-92
    • Matsudaira, P.1
  • 27
    • 0031822886 scopus 로고    scopus 로고
    • The single CH domain of calponin is neither sufficient nor necessary for F-actin binding
    • Gimona M., and Mital R. The single CH domain of calponin is neither sufficient nor necessary for F-actin binding J. Cell Sci. 111 1998 1813 1821 (Pubitemid 28370526)
    • (1998) Journal of Cell Science , vol.111 , Issue.13 , pp. 1813-1821
    • Gimona, M.1    Mital, R.2
  • 28
    • 33646182429 scopus 로고    scopus 로고
    • The CH-domain of calponin does not determine the modes of calponin binding to F-actin
    • Galkin V.E., Orlova A., Fattoum A., Walsh M.P., and Egelman E.H. The CH-domain of calponin does not determine the modes of calponin binding to F-actin J. Mol. Biol. 359 2006 478 485
    • (2006) J. Mol. Biol. , vol.359 , pp. 478-485
    • Galkin, V.E.1    Orlova, A.2    Fattoum, A.3    Walsh, M.P.4    Egelman, E.H.5
  • 32
    • 0141843643 scopus 로고    scopus 로고
    • Elechron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • DOI 10.1038/nature02005
    • Holmes K.C., Angert I., Kull F.J., Jahn W., and Schroder R.R. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide Nature 425 2003 423 427 (Pubitemid 37187274)
    • (2003) Nature , vol.425 , Issue.6956 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schroder, R.R.5
  • 33
    • 33744993933 scopus 로고    scopus 로고
    • Activation of myocardial contraction by the N-terminal domains of myosin binding protein-C
    • DOI 10.1161/01.RES.0000222059.54917.ef, PII 0000301220060526000011
    • Herron T.J., Rostkova E., Kunst G., Chaturvedi R., Gautel M., and Kentish J.C. Activation of myocardial contraction by the N-terminal domains of myosin binding protein-C Circ. Res. 98 2006 1290 1298 (Pubitemid 43948084)
    • (2006) Circulation Research , vol.98 , Issue.10 , pp. 1290-1298
    • Herron, T.J.1    Rostkova, E.2    Kunst, G.3    Chaturvedi, R.4    Gautel, M.5    Kentish, J.C.6
  • 34
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I., Holden H.M., Whittaker M., Yohn C.B., Lorenz M., Holmes K.C., and Milligan R.A. Structure of the actin-myosin complex and its implications for muscle contraction Science 261 1993 58 65 (Pubitemid 23265380)
    • (1993) Science , vol.261 , Issue.5117 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3    Yohn, C.B.4    Lorenz, M.5    Holmes, K.C.6    Milligan, R.A.7
  • 35
    • 0026593988 scopus 로고
    • Actomyosin interactions in the presence of ATP and the N-terminal segment of actin
    • DasGupta G., and Reisler E. Actomyosin interactions in the presence of ATP and the N-terminal segment of actin Biochemistry 31 1992 1836 1841
    • (1992) Biochemistry , vol.31 , pp. 1836-1841
    • Dasgupta, G.1    Reisler, E.2
  • 36
    • 0025938170 scopus 로고
    • Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: Detection by antibodies against the N-terminal segment of actin
    • DasGupta G., and Reisler E. Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: detection by antibodies against the N-terminal segment of actin Biochemistry 30 1991 9961 9966
    • (1991) Biochemistry , vol.30 , pp. 9961-9966
    • Dasgupta, G.1    Reisler, E.2
  • 37
    • 44649152239 scopus 로고    scopus 로고
    • Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay
    • Saber W., Begin K.J., Warshaw D.M., and VanBuren P. Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay J. Mol. Cell. Cardiol. 44 2008 1053 1061
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 1053-1061
    • Saber, W.1    Begin, K.J.2    Warshaw, D.M.3    Vanburen, P.4
  • 39
    • 0024974811 scopus 로고
    • Antibody against the amino terminus of δ-actin inhibits actomyosin interactions in the presence of ATP
    • DasGupta G., and Reisler E. Antibody against the amino terminus of δ-actin inhibits actomyosin interactions in the presence of ATP J. Mol. Biol. 207 1989 833 836
    • (1989) J. Mol. Biol. , vol.207 , pp. 833-836
    • Dasgupta, G.1    Reisler, E.2
  • 40
    • 0036214903 scopus 로고    scopus 로고
    • A model of cross-bridge attachment to actin in the AMATP state based on x-ray diffraction from permeabilized rabbit psoas muscle
    • Gu J., Xu S., and Yu L.C. A model of cross-bridge attachment to actin in the A*M*ATP state based on X-ray diffraction from permeabilized rabbit psoas muscle Biophys. J. 82 2002 2123 2133 (Pubitemid 34280825)
    • (2002) Biophysical Journal , vol.82 , Issue.4 , pp. 2123-2133
    • Gu, J.1    Xu, S.2    Yu, L.C.3
  • 41
    • 33846021648 scopus 로고    scopus 로고
    • Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: Evidence for long-lived cross-bridges
    • DOI 10.1074/jbc.M606949200
    • Razumova M.V., Shaffer J.F., Tu A.Y., Flint G.V., Regnier M., and Harris S.P. Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: evidence for long-lived cross-bridges J. Biol. Chem. 281 2006 35846 35854 (Pubitemid 46041316)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35846-35854
    • Razumova, M.V.1    Shaffer, J.F.2    Tu, A.-Y.3    Flint, G.V.4    Regnier, M.5    Harris, S.P.6
  • 42
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • DOI 10.1006/jsbi.1996.0030
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199 (Pubitemid 26093143)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 43
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97 (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 44
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods Ultramicroscopy 85 2000 225 234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 45
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of β-actin at 2.65 A resolution
    • DOI 10.1006/jmbi.1996.0602
    • Chik J.K., Lindberg U., and Schutt C.E. The structure of an open state of β-actin at 2.65 angstrom resolution J. Mol. Biol. 263 1996 607 623 (Pubitemid 26382079)
    • (1996) Journal of Molecular Biology , vol.263 , Issue.4 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.