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Volumn 23, Issue 12, 2009, Pages 4117-4125

Nebulin plays a direct role in promoting strong actin-myosin interactions

Author keywords

Cytoskeletal proteins; Muscle force generation; Muscle performance

Indexed keywords

ACTIN; CALCIUM ION; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; NEBULIN;

EID: 72749126316     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-137729     Document Type: Article
Times cited : (61)

References (43)
  • 1
    • 0026101389 scopus 로고
    • Nebulin as a giant actin-binding template protein in skeletal muscle sarcomere. Interaction of actin and cloned human nebulin fragments
    • Jin, J. P., and Wang, K. (1991) Nebulin as a giant actin-binding template protein in skeletal muscle sarcomere. Interaction of actin and cloned human nebulin fragments. FEBS Lett. 281, 93-96
    • (1991) FEBS Lett. , vol.281 , pp. 93-96
    • Jin, J.P.1    Wang, K.2
  • 2
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl, M., Winder, S. J., and Pastore, A. (1994) Nebulin, a helical actin binding protein. EMBO J. 13, 1782-1789 (Pubitemid 24124510)
    • (1994) EMBO Journal , vol.13 , Issue.8 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 3
    • 0030039635 scopus 로고    scopus 로고
    • Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3
    • DOI 10.1074/jbc.271.8.4304
    • Wang, K., Knipfer, M., Huang, Q. Q., van Heerden, A., Hsu, L. C., Gutierrez, G., Quian, X. L., and Stedman, H. (1996) Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture: sequence motifs and affinity profiles of tandem repeats and terminal SH3. J. Biol. Chem. 271, 4304-4314 (Pubitemid 26070537)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4304-4314
    • Wang, K.1    Knipfer, M.2    Huang, Q.-Q.3    Van Heerden, A.4    Hsu, L.C.-L.5    Gutierrez, G.6    Quian, X.-L.7    Stedman, H.8
  • 4
    • 0034976418 scopus 로고    scopus 로고
    • Actin dynamics at pointed ends regulates thin filament length in striated muscle
    • DOI 10.1038/35078517
    • Littlefield, R., Almenar-Queralt, A., and Fowler, V. M. (2001) Actin dynamics at pointed ends regulates thin filament length in striated muscle. Nat. Cell Biol. 3, 544-551 (Pubitemid 32536850)
    • (2001) Nature Cell Biology , vol.3 , Issue.6 , pp. 544-551
    • Littlefield, R.1    Almenar-Queralt, A.2    Fowler, V.M.3
  • 5
    • 0035808418 scopus 로고    scopus 로고
    • The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments
    • DOI 10.1074/jbc.M005693200
    • McElhinny, A. S., Kolmerer, B., Fowler, V. M., Labeit, S., and Gregorio, C. C. (2001) The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments. J. Biol. Chem. 276, 583-592 (Pubitemid 32050355)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 583-592
    • McElhinny, A.S.1    Kolmerer, B.2    Fowler, V.M.3    Labeit, S.4    Gregorio, C.C.5
  • 6
    • 0028891855 scopus 로고
    • Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments
    • Schafer, D. A., Hug, C., and Cooper, J. A. (1995) Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments. J. Cell Biol. 128, 61-70
    • (1995) J. Cell Biol. , vol.128 , pp. 61-70
    • Schafer, D.A.1    Hug, C.2    Cooper, J.A.3
  • 7
    • 0023372284 scopus 로고
    • Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • Casella, J. F., Craig, S. W., Maack, D. J., and Brown, A. E. (1987) Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J. Cell Biol. 105, 371-379
    • (1987) J. Cell Biol. , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 8
    • 18744397819 scopus 로고    scopus 로고
    • Molecular dissection of the interaction of desmin with the C-terminal region of nebulin
    • DOI 10.1006/jsbi.2002.4457
    • Bang, M. L., Gregorio, C., and Labeit, S. (2002) Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J. Struct. Biol. 137, 119-127 (Pubitemid 35430427)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 119-127
    • Bang, M.-L.1    Gregorio, C.2    Labeit, S.3
  • 9
    • 33748058496 scopus 로고    scopus 로고
    • Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo
    • DOI 10.1038/sj.emboj.7601242, PII 7601242
    • Witt, C. C., Burkart, C., Labeit, D., McNabb, M., Wu, Y., Granzier, H., and Labeit, S. (2006) Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J. 25, 3843-3855 (Pubitemid 44300270)
    • (2006) EMBO Journal , vol.25 , Issue.16 , pp. 3843-3855
    • Witt, C.C.1    Burkart, C.2    Labeit, D.3    McNabb, M.4    Wu, Y.5    Granzier, H.6    Labeit, S.7
  • 10
    • 0037132502 scopus 로고    scopus 로고
    • Interaction of nebulin SH3 domain with titin PEVK and myopalladin: Implications for the signaling and assembly role of titin and nebulin
    • DOI 10.1016/S0014-5793(02)03655-4, PII S0014579302036554
    • Ma, K., and Wang, K. (2002) Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin. FEBS Lett. 532, 273-278 (Pubitemid 35441360)
    • (2002) FEBS Letters , vol.532 , Issue.3 , pp. 273-278
    • Ma, K.1    Wang, K.2
  • 12
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit, S., and Kolmerer, B. (1995) The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 248, 308-315
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 14
    • 33745243854 scopus 로고    scopus 로고
    • Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
    • DOI 10.1083/jcb.200603119
    • Bang, M. L., Li, X., Littlefield, R., Bremner, S., Thor, A., Knowlton, K. U., Lieber, R. L., and Chen, J. (2006) Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. J. Cell Biol. 173, 905-916 (Pubitemid 43920698)
    • (2006) Journal of Cell Biology , vol.173 , Issue.6 , pp. 905-916
    • Bang, M.-L.1    Li, X.2    Littlefield, R.3    Bremner, S.4    Thor, A.5    Knowlton, K.U.6    Lieber, R.L.7    Chen, J.8
  • 17
    • 0035814795 scopus 로고    scopus 로고
    • High-affinity actin-binding nebulin fragments influence the actoS1 complex
    • Root, D. D., and Wang, K. (2001) High-affinity actin-binding nebulin fragments influence the actoS1 complex. Biochemistry 40, 1171-1186
    • (2001) Biochemistry , vol.40 , pp. 1171-1186
    • Root, D.D.1    Wang, K.2
  • 18
    • 0028080839 scopus 로고
    • Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin
    • Root, D. D., and Wang, K. (1994) Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin. Biochemistry 33, 12581-12591
    • (1994) Biochemistry , vol.33 , pp. 12581-12591
    • Root, D.D.1    Wang, K.2
  • 20
    • 0036231585 scopus 로고    scopus 로고
    • Measurement of thin filament lengths by distributed deconvolution analysis of fluorescence images
    • Littlefield, R., and Fowler, V. M. (2002) Measurement of thin filament lengths by distributed deconvolution analysis of fluorescence images. Biophys. J. 82, 2548-2564 (Pubitemid 34441294)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2548-2564
    • Littlefield, R.1    Fowler, V.M.2
  • 21
    • 0025690381 scopus 로고
    • The contractile response during steady lengthening of stimulated frog muscle fibres
    • Lombardi, V., and Piazzesi, G. (1990) The contractile response during steady lengthening of stimulated frog muscle fibres. J. Physiol. 431, 141-171
    • (1990) J. Physiol. , vol.431 , pp. 141-171
    • Lombardi, V.1    Piazzesi, G.2
  • 22
    • 0002840114 scopus 로고
    • A sensitive force transducer with resonant frequency 50 kHz
    • Huxley, A. F., and Lombardi, V. (1980) A sensitive force transducer with resonant frequency 50 kHz. J. Physiol. 305, 15P-16P
    • (1980) J. Physiol. , vol.305
    • Huxley, A.F.1    Lombardi, V.2
  • 23
    • 34047208553 scopus 로고    scopus 로고
    • Stiffness and fraction of myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas
    • DOI 10.1529/biophysj.106.099549
    • Linari, M., Caremani, M., Piperio, C., Brandt, P., and Lombardi, V. (2007) Stiffness and fraction of myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas. Biophys. J. 92, 2476-2490 (Pubitemid 46536429)
    • (2007) Biophysical Journal , vol.92 , Issue.7 , pp. 2476-2490
    • Linari, M.1    Caremani, M.2    Piperio, C.3    Brandt, P.4    Lombardi, V.5
  • 24
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres
    • Dantzig, J. A., Goldman, Y. E., Millar, N. C., Lacktis, J., and Homsher, E. (1992) Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J. Physiol. 451, 247-278
    • (1992) J. Physiol. , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Lacktis, J.4    Homsher, E.5
  • 25
    • 0021284583 scopus 로고
    • Relaxation of rabbit psoas muscle fibres from rigor by photochemical generation of adenosine-5′-triphosphate
    • Goldman, Y. E., Hibberd, M. G., and Trentham, D. R. (1984) Relaxation of rabbit psoas muscle fibres from rigor by photochemical generation of adenosine-5′-triphosphate. J. Physiol. 354, 577-604
    • (1984) J. Physiol. , vol.354 , pp. 577-604
    • Goldman, Y.E.1    Hibberd, M.G.2    Trentham, D.R.3
  • 26
    • 0023091848 scopus 로고
    • The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers
    • DOI 10.1007/BF00581833
    • Kawai, M., Guth, K., Winnikes, K., Haist, C., and Ruegg, J. C. (1987) The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers. Pflügers Arch. 408, 1-9 (Pubitemid 17030223)
    • (1987) Pflugers Archiv European Journal of Physiology , vol.408 , Issue.1 , pp. 1-9
    • Kawai, M.1    Guth, K.2    Winnikes, K.3
  • 27
    • 0842344627 scopus 로고    scopus 로고
    • The mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoforms
    • DOI 10.1113/jphysiol.2003.051748
    • Linari, M., Bottinelli, R., Pellegrino, M. A., Reconditi, M., Reggiani, C., and Lombardi, V. (2004) The mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoforms. J. Physiol. 554, 335-352 (Pubitemid 38181348)
    • (2004) Journal of Physiology , vol.554 , Issue.2 , pp. 335-352
    • Linari, M.1    Bottinelli, R.2    Pellegrino, M.A.3    Reconditi, M.4    Reggiani, C.5    Lombardi, V.6
  • 28
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: A steady-state and transient kinetic study
    • Millar, N. C., and Homsher, E. (1990) The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: a steady-state and transient kinetic study. J. Biol. Chem. 265, 20234-20240
    • (1990) J. Biol. Chem. , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 29
    • 0029177764 scopus 로고
    • Regulation of the cross-bridge transition from a weakly to strongly bound state in skinned rabbit muscle fibers
    • Regnier, M., Morris, C., and Homsher, E. (1995) Regulation of the cross-bridge transition from a weakly to strongly bound state in skinned rabbit muscle fibers. Am. J. Physiol. 269, C1532-C1539 (Pubitemid 3020577)
    • (1995) The American Journal of Physiology , vol.269 , Issue.61
    • Regnier, M.1    Morris, C.2    Homsher, E.3
  • 30
    • 15844429778 scopus 로고    scopus 로고
    • The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle
    • DOI 10.1113/jphysiol.2004.078873
    • Sleep, J., Irving, M., and Burton, K. (2005) The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle. J. Physiol. 563, 671-687 (Pubitemid 40425588)
    • (2005) Journal of Physiology , vol.563 , Issue.3 , pp. 671-687
    • Sleep, J.1    Irving, M.2    Burton, K.3
  • 31
    • 0034008022 scopus 로고    scopus 로고
    • Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: Implications for cross-bridge action during maximum velocity of filament sliding
    • Stehle, R., and Brenner, B. (2000) Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding. Biophys. J. 78, 1458-1473 (Pubitemid 30141570)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1458-1473
    • Stehle, R.1    Brenner, B.2
  • 32
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. U. S. A. 85, 3265-3269
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 33
    • 0001145764 scopus 로고
    • The combinations of haemoglobin with oxygen and with carbon monoxide. I
    • Hill, A. V. (1913) The combinations of haemoglobin with oxygen and with carbon monoxide. I. Biochem. J. 7, 471-480
    • (1913) Biochem. J , vol.7 , pp. 471-480
    • Hill, A.V.1
  • 34
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., Homsher, E., and Regnier, M. (2000) Regulation of contraction in striated muscle. Physiol. Rev. 80, 853-924
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 35
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and Simmons, R. M. (1971) Proposed mechanism of force generation in striated muscle. Nature 233, 533-538
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 36
    • 33845326726 scopus 로고    scopus 로고
    • Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: Stiffness and X-ray diffraction measurements
    • DOI 10.1113/jphysiol.2006.115394
    • Brunello, E., Bianco, P., Piazzesi, G., Linari, M., Reconditi, M., Panine, P., Narayanan, T., Helsby, W. I., Irving, M., and Lombardi, V. (2006) Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurements. J. Physiol. 577, 971-984 (Pubitemid 44873659)
    • (2006) Journal of Physiology , vol.577 , Issue.3 , pp. 971-984
    • Brunello, E.1    Bianco, P.2    Piazzesi, G.3    Linari, M.4    Reconditi, M.5    Panine, P.6    Narayanan, T.7    Helsby, W.I.8    Irving, M.9    Lombardi, V.10
  • 37
    • 36148935250 scopus 로고    scopus 로고
    • Skeletal Muscle Performance Determined by Modulation of Number of Myosin Motors Rather Than Motor Force or Stroke Size
    • DOI 10.1016/j.cell.2007.09.045, PII S0092867407012895
    • Piazzesi, G., Reconditi, M., Linari, M., Lucii, L., Bianco, P., Brunello, E., Decostre, V., Stewart, A., Gore, D. B., Irving, T. C., Irving, M., and Lombardi, V. (2007) Skeletal muscle performance determined by modulation of number of myosin motors rather than motor force or stroke size. Cell 131, 784-795 (Pubitemid 350103598)
    • (2007) Cell , vol.131 , Issue.4 , pp. 784-795
    • Piazzesi, G.1    Reconditi, M.2    Linari, M.3    Lucii, L.4    Bianco, P.5    Brunello, E.6    Decostre, V.7    Stewart, A.8    Gore, D.B.9    Irving, T.C.10    Irving, M.11    Lombardi, V.12
  • 38
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. (1957) Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7, 255-318
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 39
    • 0018333803 scopus 로고
    • The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres
    • Edman, K. A. (1979) The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J. Physiol. 291, 143-159
    • (1979) J. Physiol. , vol.291 , pp. 143-159
    • Edman, K.A.1
  • 40
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of muscle
    • Hill, A. V. (1938) The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. Lond. B Biol. Sci. 126, 136-195
    • (1938) Proc. R. Soc. Lond. B Biol. Sci. , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 42
    • 0002639024 scopus 로고
    • Mechanics and models of muscular contraction
    • Linden, R. J., ed p Churchill Livingstone, London
    • Simmons, R. M., and Jewell, B. R. (1974) Mechanics and models of muscular contraction. In Recent Advances in Physiology, Vol.9 (Linden, R. J., ed) pp. 87-147, Churchill Livingstone, London
    • (1974) Recent Advances in Physiology , vol.9 , pp. 87-147
    • Simmons, R.M.1    Jewell, B.R.2
  • 43
    • 0022557260 scopus 로고
    • Calcium and strontium activation of single skinned muscle fibres of normal and dystrophic mice
    • Fink, R. H., Stephenson, D. G., and Williams, D. A. (1986) Calcium and strontium activation of single skinned muscle fibres of normal and dystrophic mice. J. Physiol. 373, 513-525
    • (1986) J. Physiol. , vol.373 , pp. 513-525
    • Fink, R.H.1    Stephenson, D.G.2    Williams, D.A.3


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