메뉴 건너뛰기




Volumn 1804, Issue 9, 2010, Pages 1796-1809

A biophysical map of the dystrophin rod

Author keywords

Domain; Dystrophin; Spectrin type repeat; Stability

Indexed keywords

DYSTROPHIN; NITRIC OXIDE SYNTHASE; SPECTRIN; ACTIN; NEURONAL NITRIC OXIDE SYNTHASE;

EID: 77955095972     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.03.009     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, alpha-actinin, and dystrophin
    • Broderick M.J., Winder S.J. Spectrin, alpha-actinin, and dystrophin. Adv. Protein Chem. 2005, 70:203-246.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 203-246
    • Broderick, M.J.1    Winder, S.J.2
  • 2
    • 33846271135 scopus 로고    scopus 로고
    • Dystrophin, its interactions with other proteins, and implications for muscular dystrophy
    • Ervasti J.M. Dystrophin, its interactions with other proteins, and implications for muscular dystrophy. Biochim. Biophys. Acta 2007, 1772:108-117.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 108-117
    • Ervasti, J.M.1
  • 3
    • 0022599356 scopus 로고
    • The present status of erythrocyte spectrin structure: the 106-residue repetitive structure is a basic feature of an entire class of proteins
    • Speicher D.W. The present status of erythrocyte spectrin structure: the 106-residue repetitive structure is a basic feature of an entire class of proteins. J. Cell. Biochem. 1986, 30:245-258.
    • (1986) J. Cell. Biochem. , vol.30 , pp. 245-258
    • Speicher, D.W.1
  • 4
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher D.W., Marchesi V.T. Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 1984, 311:177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 5
    • 0026510756 scopus 로고
    • Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins
    • Parry D.A., Dixon T.W., Cohen C. Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins. Biophys. J. 1992, 61:858-867.
    • (1992) Biophys. J. , vol.61 , pp. 858-867
    • Parry, D.A.1    Dixon, T.W.2    Cohen, C.3
  • 6
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: a family of versatile cytolinker proteins
    • Leung C.L., Green K.J., Liem R.K. Plakins: a family of versatile cytolinker proteins. Trends Cell Biol. 2002, 12:37-45.
    • (2002) Trends Cell Biol. , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liem, R.K.3
  • 7
    • 0030795164 scopus 로고    scopus 로고
    • The plakin family: versatile organizers of cytoskeletal architecture
    • Ruhrberg C., Watt F.M. The plakin family: versatile organizers of cytoskeletal architecture. Curr. Opin. Genet. Dev. 1997, 7:392-397.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 392-397
    • Ruhrberg, C.1    Watt, F.M.2
  • 9
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum V.L., Li D., MacDonald R.I., Mondragon A. Structures of two repeats of spectrin suggest models of flexibility. Cell 1999, 98:523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 11
    • 17444366419 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod: four spectrin repeats forming a thight dimer
    • Ylanne J., Scheffzek K., Young P., Saraste M. Crystal structure of the alpha-actinin rod: four spectrin repeats forming a thight dimer. Cell. Mol. Biol. Lett. 2001, 6:234.
    • (2001) Cell. Mol. Biol. Lett. , vol.6 , pp. 234
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 13
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo K., Young P., Gautel M., Saraste M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 1999, 98:537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 14
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil
    • Pascual J., Pfuhl M., Walther D., Saraste M., Nilges M. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J. Mol. Biol. 1997, 273:740-751.
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 15
    • 0034680758 scopus 로고    scopus 로고
    • NMR analysis of secondary structure and dynamics of a recombinant peptide from the N-terminal region of human erythroid alpha-spectrin
    • Park S., Johnson M.E., Fung L.W. NMR analysis of secondary structure and dynamics of a recombinant peptide from the N-terminal region of human erythroid alpha-spectrin. FEBS Lett. 2000, 485:81-86.
    • (2000) FEBS Lett. , vol.485 , pp. 81-86
    • Park, S.1    Johnson, M.E.2    Fung, L.W.3
  • 16
    • 53149120329 scopus 로고    scopus 로고
    • Stability of dystrophin STR fragments in relation to junction helicity
    • Mirza A., Menhart N. Stability of dystrophin STR fragments in relation to junction helicity. Biochim. Biophys. Acta 2008, 1784:1301-1309.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1301-1309
    • Mirza, A.1    Menhart, N.2
  • 17
    • 0030975421 scopus 로고    scopus 로고
    • Physical properties of a single-motif erythrocyte spectrin peptide: a highly stable independently folding unit
    • DeSilva T.M., Harper S.L., Kotula L., Hensley P., Curtis P.J., Otvos L., Speicher D.W. Physical properties of a single-motif erythrocyte spectrin peptide: a highly stable independently folding unit. Biochemistry 1997, 36:3991-3997.
    • (1997) Biochemistry , vol.36 , pp. 3991-3997
    • DeSilva, T.M.1    Harper, S.L.2    Kotula, L.3    Hensley, P.4    Curtis, P.J.5    Otvos, L.6    Speicher, D.W.7
  • 18
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles
    • Rief M., Pascual J., Saraste M., Gaub H.E. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 1999, 286:553-561.
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 19
    • 0028372220 scopus 로고
    • Spectrin motif. Conformation of a mammoth protein
    • Speicher D.W., Ursitti J.A. Spectrin motif. Conformation of a mammoth protein. Curr. Biol. 1994, 4:154-157.
    • (1994) Curr. Biol. , vol.4 , pp. 154-157
    • Speicher, D.W.1    Ursitti, J.A.2
  • 20
    • 0025234309 scopus 로고
    • Structural predictions for the central domain of dystrophin
    • Cross R.A., Stewart M., Kendrick-Jones J. Structural predictions for the central domain of dystrophin. FEBS Lett. 1990, 262:87-92.
    • (1990) FEBS Lett. , vol.262 , pp. 87-92
    • Cross, R.A.1    Stewart, M.2    Kendrick-Jones, J.3
  • 22
    • 0029825450 scopus 로고    scopus 로고
    • Peptides with more than one 106-amino acid sequence motif are needed to mimic the structural stability of spectrin
    • Menhart N., Mitchell T., Lusitani D., Topouzian N., Fung L.W. Peptides with more than one 106-amino acid sequence motif are needed to mimic the structural stability of spectrin. J. Biol. Chem. 1996, 271:30410-30416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30410-30416
    • Menhart, N.1    Mitchell, T.2    Lusitani, D.3    Topouzian, N.4    Fung, L.W.5
  • 23
    • 33646524933 scopus 로고    scopus 로고
    • Structural cooperativity in spectrin type repeats motifs of dystrophin
    • Saadat L., Pittman L., Menhart N. Structural cooperativity in spectrin type repeats motifs of dystrophin. Biochim. Biophys. Acta 2006, 1764:943-954.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 943-954
    • Saadat, L.1    Pittman, L.2    Menhart, N.3
  • 24
    • 33646135074 scopus 로고    scopus 로고
    • Extending a spectrin repeat unit. II: rupture behavior
    • Paramore S., Ayton G.S., Voth G.A. Extending a spectrin repeat unit. II: rupture behavior. Biophys. J. 2006, 90:101-111.
    • (2006) Biophys. J. , vol.90 , pp. 101-111
    • Paramore, S.1    Ayton, G.S.2    Voth, G.A.3
  • 25
    • 33646675371 scopus 로고    scopus 로고
    • Dissecting the signaling and mechanical functions of the dystrophin-glycoprotein complex
    • Judge L.M., Haraguchiln M., Chamberlain J.S. Dissecting the signaling and mechanical functions of the dystrophin-glycoprotein complex. J. Cell Sci. 2006, 119:1537-1546.
    • (2006) J. Cell Sci. , vol.119 , pp. 1537-1546
    • Judge, L.M.1    Haraguchiln, M.2    Chamberlain, J.S.3
  • 26
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova I.N., Patel J.R., Ervasti J.M. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol. 2000, 150:1209-1214.
    • (2000) J. Cell Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 27
    • 63349112286 scopus 로고    scopus 로고
    • Systemic human minidystrophin gene transfer improves functions and life span of dystrophin and dystrophin/utrophin-deficient mice
    • Wang B., Li J., Fu F.H., Xiao X. Systemic human minidystrophin gene transfer improves functions and life span of dystrophin and dystrophin/utrophin-deficient mice. J. Orthop. Res. 2009, 27:421-426.
    • (2009) J. Orthop. Res. , vol.27 , pp. 421-426
    • Wang, B.1    Li, J.2    Fu, F.H.3    Xiao, X.4
  • 28
    • 66149123674 scopus 로고    scopus 로고
    • Gene therapy in large animal models of muscular dystrophy, ILAR journal / National Research Council, Institute of Laboratory Animal Resources 50
    • Z. Wang, J.S. Chamberlain, S.J. Tapscott, R. Storb, Gene therapy in large animal models of muscular dystrophy, ILAR journal / National Research Council, Institute of Laboratory Animal Resources 50 (2009) 187-198.
    • (2009) , pp. 187-198
    • Wang Z., J.S.1    Chamberlain, S.J.2    Tapscott Storb, R.3
  • 31
    • 33744507184 scopus 로고    scopus 로고
    • Dystrophin and utrophin bind actin through distinct modes of contact
    • Rybakova I.N., Humston J.L., Sonnemann K.J., Ervasti J.M. Dystrophin and utrophin bind actin through distinct modes of contact. J. Biol. Chem. 2006, 281:9996-10001.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9996-10001
    • Rybakova, I.N.1    Humston, J.L.2    Sonnemann, K.J.3    Ervasti, J.M.4
  • 33
    • 0025217703 scopus 로고
    • Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility
    • Koenig M., Kunkel L.M. Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. J. Biol. Chem. 1990, 265:4560-4566.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4560-4566
    • Koenig, M.1    Kunkel, L.M.2
  • 36
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N., Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969, 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 37
    • 33745215797 scopus 로고    scopus 로고
    • Hybrid spectrin type repeats produced by exon-skipping in dystrophin
    • Menhart N. Hybrid spectrin type repeats produced by exon-skipping in dystrophin. Biochim. Biophys. Acta 2006, 1764:993-999.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 993-999
    • Menhart, N.1
  • 38
    • 67349085538 scopus 로고    scopus 로고
    • Differential stabilities of alternative exon-skipped rod motifs of dystrophin
    • Ruszczak C., Mirza A., Menhart N. Differential stabilities of alternative exon-skipped rod motifs of dystrophin. Biochim. Biophys. Acta 2009, 1794:921-928.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 921-928
    • Ruszczak, C.1    Mirza, A.2    Menhart, N.3
  • 39
    • 0029758344 scopus 로고    scopus 로고
    • Stability of the dystrophin rod domain fold: evidence for nested repeating units
    • Calvert R., Kahana E., Gratzer W.B. Stability of the dystrophin rod domain fold: evidence for nested repeating units. Biophys. J. 1996, 71:1605-1610.
    • (1996) Biophys. J. , vol.71 , pp. 1605-1610
    • Calvert, R.1    Kahana, E.2    Gratzer, W.B.3
  • 40
    • 33748742268 scopus 로고    scopus 로고
    • Is any measurement method optimal for all aggregate sizes and types?
    • Philo J.S. Is any measurement method optimal for all aggregate sizes and types?. AAPS J. 2006, 8:E564-571.
    • (2006) AAPS J. , vol.8
    • Philo, J.S.1
  • 44
    • 0036667981 scopus 로고    scopus 로고
    • Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable
    • Harper S.Q., Crawford R.W., DelloRusso C., Chamberlain J.S. Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable. Hum. Mol. Genet. 2002, 11:1807-1815.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1807-1815
    • Harper, S.Q.1    Crawford, R.W.2    DelloRusso, C.3    Chamberlain, J.S.4
  • 46
    • 0032561199 scopus 로고    scopus 로고
    • A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction
    • Amann K.J., Renley B.A., Ervasti J.M. A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction. J. Biol. Chem. 1998, 273:28419-28423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28419-28423
    • Amann, K.J.1    Renley, B.A.2    Ervasti, J.M.3
  • 47
    • 65649111197 scopus 로고    scopus 로고
    • Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy
    • Lai Y., Thomas G.D., Yue Y., Yang H.T., Li D., Long C., Judge L., Bostick B., Chamberlain J.S., Terjung R.L., Duan D. Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy. J. Clin. Invest. 2009, 119:624-635.
    • (2009) J. Clin. Invest. , vol.119 , pp. 624-635
    • Lai, Y.1    Thomas, G.D.2    Yue, Y.3    Yang, H.T.4    Li, D.5    Long, C.6    Judge, L.7    Bostick, B.8    Chamberlain, J.S.9    Terjung, R.L.10    Duan, D.11
  • 49
    • 65849498675 scopus 로고    scopus 로고
    • A two-amino acid mutation encountered in duchenne muscular dystrophy decreases stability of the rod domain 23 (R23) spectrin-like repeat of dystrophin
    • Legardinier S., Legrand B., Raguenes-Nicol C., Bondon A., Hardy S., Tascon C., Le Rumeur E., Hubert J.F. A two-amino acid mutation encountered in duchenne muscular dystrophy decreases stability of the rod domain 23 (R23) spectrin-like repeat of dystrophin. J. Biol. Chem. 2009, 284:8822-8832.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8822-8832
    • Legardinier, S.1    Legrand, B.2    Raguenes-Nicol, C.3    Bondon, A.4    Hardy, S.5    Tascon, C.6    Le Rumeur, E.7    Hubert, J.F.8
  • 50
    • 1242319561 scopus 로고    scopus 로고
    • Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer
    • MacDonald R.I., Cummings J.A. Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:1502-1507.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1502-1507
    • MacDonald, R.I.1    Cummings, J.A.2
  • 51
    • 0029063876 scopus 로고
    • Minimum folding unit of dystrophin rod domain
    • Kahana E., Gratzer W.B. Minimum folding unit of dystrophin rod domain. Biochemistry 1995, 34:8110-8114.
    • (1995) Biochemistry , vol.34 , pp. 8110-8114
    • Kahana, E.1    Gratzer, W.B.2
  • 52
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
    • Ylanne J., Scheffzek K., Young P., Saraste M. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure (Camb) 2001, 9:597-604.
    • (2001) Structure (Camb) , vol.9 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.