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Volumn 106, Issue 19, 2009, Pages 7822-7827

Dystrophin and utrophin have distinct effects on the structural dynamics of actin

Author keywords

Flexibility; Muscular dystrophy; Phosphorescence; Spectroscopy

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; DYE; DYSTROPHIN; IRON; STEEL; UTROPHIN;

EID: 66049139116     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0812007106     Document Type: Article
Times cited : (39)

References (27)
  • 1
    • 0026453372 scopus 로고
    • Direct visualization of the dystrophin network on skeletal muscle fiber membrane
    • Straub V, Bittner RE, Leger JJ, Voit T (1992) Direct visualization of the dystrophin network on skeletal muscle fiber membrane. J Cell Biol 119:1183-1191.
    • (1992) J Cell Biol , vol.119 , pp. 1183-1191
    • Straub, V.1    Bittner, R.E.2    Leger, J.J.3    Voit, T.4
  • 2
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: The Achilles' heel of Herculean muscle
    • Ervasti JM (2003) Costameres: The Achilles' heel of Herculean muscle. J Biol Chem 278:13591-13594.
    • (2003) J Biol Chem , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 3
    • 58149240131 scopus 로고    scopus 로고
    • Gene-mediated restoration of normal myofiber elasticity in dystrophic muscles
    • Puttini, et al. (2008). Gene-mediated restoration of normal myofiber elasticity in dystrophic muscles. Mol Ther 17:19-25.
    • (2008) Mol Ther , vol.17 , pp. 19-25
    • Puttini1
  • 5
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova IN, Patel JR, Ervasti JM (2000) The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J Cell Biol 150:1209-1214.
    • (2000) J Cell Biol , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 6
    • 0028833396 scopus 로고
    • Utrophin actin-binding domain: Analysis of actin binding and cellular targeting
    • Winder SJ, et al. (1995) Utrophin actin-binding domain: Analysis of actin binding and cellular targeting. J Cell Sci 108:63-71.
    • (1995) J Cell Sci , vol.108 , pp. 63-71
    • Winder, S.J.1
  • 7
    • 0031727771 scopus 로고    scopus 로고
    • Expression of full-length utrophin prevents muscular dystrophy in mdx mice
    • Tinsley J, et al. (1998) Expression of full-length utrophin prevents muscular dystrophy in mdx mice. Nat Med 4:1441-1444.
    • (1998) Nat Med , vol.4 , pp. 1441-1444
    • Tinsley, J.1
  • 8
    • 0035999982 scopus 로고    scopus 로고
    • Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle
    • DOI 10.1091/mbc.01-09-0446
    • Rybakova IN, Patel JR, Davies KE, Yurchenco PD, Ervasti JM (2002) Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle. Mol Biol Cell 13:1512-1521. (Pubitemid 34522635)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.5 , pp. 1512-1521
    • Rybakova, I.N.1    Patel, J.R.2    Davies, K.E.3    Yurchenco, P.D.4    Ervasti, J.M.5
  • 10
    • 33846271135 scopus 로고    scopus 로고
    • Dystrophin, its interactions with other proteins, and implications for muscular dystrophy
    • DOI 10.1016/j.bbadis.2006.05.010, PII S0925443906001037
    • Ervasti JM (2007) Dystrophin, its interactions with other proteins, and implications for muscular dystrophy. Biochim Biophys Acta 1772:108-117. (Pubitemid 46123911)
    • (2007) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1772 , Issue.2 , pp. 108-117
    • Ervasti, J.M.1
  • 11
    • 0037092046 scopus 로고    scopus 로고
    • The utrophin actin-binding domain binds F-actin in two different modes: Implications for the spectrin superfamily of proteins
    • Galkin VE, et al. (2002) The utrophin actin-binding domain binds F-actin in two different modes: Implications for the spectrin superfamily of proteins. J Cell Biol 157:243-251.
    • (2002) J Cell Biol , vol.157 , pp. 243-251
    • Galkin, V.E.1
  • 12
    • 0038554286 scopus 로고    scopus 로고
    • An atomic model for actin binding by the CH domains and spectrin-repeat modules of utrophin and dystrophin
    • Sutherland-Smith AJ, et al. (2003) An atomic model for actin binding by the CH domains and spectrin-repeat modules of utrophin and dystrophin. J Mol Biol 329:15-33.
    • (2003) J Mol Biol , vol.329 , pp. 15-33
    • Sutherland-Smith, A.J.1
  • 13
    • 0029966678 scopus 로고    scopus 로고
    • Microsecond rotational dynamics of actin: Spectroscopic detection and theoretical simulation
    • Prochniewicz E, Zhang Q, Howard EC, Thomas DD (1996) Microsecond rotational dynamics of actin: Spectroscopic detection and theoretical simulation. J Mol Biol 255:446-457.
    • (1996) J Mol Biol , vol.255 , pp. 446-457
    • Prochniewicz, E.1    Zhang, Q.2    Howard, E.C.3    Thomas, D.D.4
  • 14
    • 0030564835 scopus 로고    scopus 로고
    • Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament
    • Prochniewicz E, Zhang Q, Janmey PA, Thomas DD (1996) Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. J Mol Biol 260:756-766.
    • (1996) J Mol Biol , vol.260 , pp. 756-766
    • Prochniewicz, E.1    Zhang, Q.2    Janmey, P.A.3    Thomas, D.D.4
  • 15
    • 27144494251 scopus 로고    scopus 로고
    • Cofilin increases the torsional flexibility and dynamics of actin filaments
    • DOI 10.1016/j.jmb.2005.09.021, PII S0022283605010776
    • Prochniewicz E, Janson N, Thomas DD, De la Cruz EM (2005) Cofilin increases the torsional flexibility and dynamics of actin filaments. J Mol Biol 353:990-1000. (Pubitemid 41503267)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.5 , pp. 990-1000
    • Prochniewicz, E.1    Janson, N.2    Thomas, D.D.3    De La Cruz, E.M.4
  • 16
    • 0030681287 scopus 로고    scopus 로고
    • Perturbations of functional interactions with myosin induce long-range allosteric and cooperative structural changes in actin
    • DOI 10.1021/bi971201r
    • Prochniewicz E, Thomas DD (1997) Perturbations of functional interactions with myosin induce long-range allosteric and cooperative structural changes in actin. Biochemistry 36:12845-12853. (Pubitemid 27465395)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 12845-12853
    • Prochniewicz, E.1    Thomas, D.D.2
  • 17
    • 4143067982 scopus 로고    scopus 로고
    • Structural dynamics of actin during active interaction with myosin: Different effects of weakly and strongly bound myosin heads
    • Prochniewicz E, Walseth TF, Thomas DD (2004) Structural dynamics of actin during active interaction with myosin: Different effects of weakly and strongly bound myosin heads. Biochemistry 43:10642-10652.
    • (2004) Biochemistry , vol.43 , pp. 10642-10652
    • Prochniewicz, E.1    Walseth, T.F.2    Thomas, D.D.3
  • 18
    • 0029804981 scopus 로고    scopus 로고
    • A new model for the interaction of dystrophin with F-actin
    • DOI 10.1083/jcb.135.3.661
    • Rybakova IN, Amann KJ, Ervasti JM (1996) A new model for the interaction of dystrophin with F-actin. J Cell Biol 135:661-672. (Pubitemid 26372923)
    • (1996) Journal of Cell Biology , vol.135 , Issue.3 , pp. 661-672
    • Rybakova, I.N.1    Amann, K.J.2    Ervasti, J.M.3
  • 19
    • 55849141926 scopus 로고    scopus 로고
    • Changes in actin structural transitions associated with oxidative inhibition of muscle contraction
    • Prochniewicz E, Spakowicz DJ, Thomas DD (2008) Changes in actin structural transitions associated with oxidative inhibition of muscle contraction. Biochemistry 47:11811-11817.
    • (2008) Biochemistry , vol.47 , pp. 11811-11817
    • Prochniewicz, E.1    Spakowicz, D.J.2    Thomas, D.D.3
  • 20
    • 0034708341 scopus 로고    scopus 로고
    • Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism
    • Moores CA, Keep NH, Kendrick-Jones J (2000) Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism. J Mol Biol 297:465-480.
    • (2000) J Mol Biol , vol.297 , pp. 465-480
    • Moores, C.A.1    Keep, N.H.2    Kendrick-Jones, J.3
  • 21
    • 0033539674 scopus 로고    scopus 로고
    • Differences in structural dynamics of muscle and yeast actin accompany differences in functional interactions with myosin
    • Prochniewicz E, Thomas DD (1999) Differences in structural dynamics of muscle and yeast actin accompany differences in functional interactions with myosin. Biochemistry 38:14860-14867. (Pubitemid 129517630)
    • (1999) Biochemistry , vol.38 , Issue.45 , pp. 14860-14867
    • Prochniewicz, E.1    Thomas, D.D.2
  • 22
    • 0018188248 scopus 로고
    • Interaction of actin with divalent cations. 1. The effect of various cations on the physical state of actin
    • Strzelecka-Golaszewska H, Prochniewicz E, Drabikowski W (1978) Interaction of actin with divalent cations. 1. The effect of various cations on the physical state of actin. Eur J Biochem 88:219-227.
    • (1978) Eur J Biochem , vol.88 , pp. 219-227
    • Strzelecka-Golaszewska, H.1    Prochniewicz, E.2    Drabikowski, W.3
  • 23
    • 0036371382 scopus 로고    scopus 로고
    • Changes in actin and myosin structural dynamics due to their weak and strong interactions
    • Thomas DD, Prochniewicz E, Roopnarine O (2002) Changes in actin and myosin structural dynamics due to their weak and strong interactions. Results Probl Cell Differ 36:7-19.
    • (2002) Results Probl Cell Differ , vol.36 , pp. 7-19
    • Thomas, D.D.1    Prochniewicz, E.2    Roopnarine, O.3
  • 25
    • 0026595121 scopus 로고
    • Binding sites involved in the interaction of actin with the N-terminal region of dystrophin
    • Levine BA, Moir AJ, Patchell VB, Perry SV (1992) Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Lett 298:44-48.
    • (1992) FEBS Lett , vol.298 , pp. 44-48
    • Levine, B.A.1    Moir, A.J.2    Patchell, V.B.3    Perry, S.V.4
  • 26
  • 27
    • 0021659708 scopus 로고
    • Microsecond rotational motions of eosin-labeled myosin measured by time-resolved anisotropy of absorption and phosphorescence
    • DOI 10.1016/0022-2836(84)90306-1
    • Eads TM, Thomas DD, Austin RH (1984) Microsecond rotational motions of eosin-labeled myosin measured by time-resolved anisotropy of absorption and phosphorescence. J Mol Biol 179:55-81. (Pubitemid 16223389)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.1 , pp. 55-81
    • Eads, T.M.1    Thomas, D.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.