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Volumn 107, Issue 49, 2010, Pages 20964-20969

Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments

Author keywords

Contraction; Cytokinesis; Macromolecular assembly

Indexed keywords

MUTANT PROTEIN; MYOSIN II;

EID: 78650486924     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1007025107     Document Type: Article
Times cited : (39)

References (38)
  • 1
    • 0034308409 scopus 로고    scopus 로고
    • Cross-bridge action: Present views, prospects, and unknowns
    • Huxley AF (2000) Cross-bridge action: Present views, prospects, and unknowns. J Biomech 33:1189-1195.
    • (2000) J Biomech , vol.33 , pp. 1189-1195
    • Huxley, A.F.1
  • 2
    • 0023484279 scopus 로고
    • Myosin structure and function in cell motility
    • Warrick HM, Spudich JA (1987) Myosin structure and function in cell motility. Annu Rev Cell Biol 3:379-421.
    • (1987) Annu Rev Cell Biol , vol.3 , pp. 379-421
    • Warrick, H.M.1    Spudich, J.A.2
  • 3
  • 4
    • 0014693726 scopus 로고
    • Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation
    • Lowey S, Slayter HS,Weeds AG, Baker H (1969) Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J Mol Biol 42:1-29.
    • (1969) J Mol Biol , vol.42 , pp. 1-29
    • Lowey, S.1    Slayter, H.S.2    Weeds, A.G.3    Baker, H.4
  • 5
    • 0019873745 scopus 로고
    • Structure of rabbit skeletal myosin. Analysis of the amino acid sequences of two fragments from the rod region
    • Parry DA (1981) Structure of rabbit skeletal myosin. Analysis of the amino acid sequences of two fragments from the rod region. J Mol Biol 153:459-464.
    • (1981) J Mol Biol , vol.153 , pp. 459-464
    • Parry, D.A.1
  • 6
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan AD, Karn J (1982) Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 299:226-231.
    • (1982) Nature , vol.299 , pp. 226-231
    • McLachlan, A.D.1    Karn, J.2
  • 7
    • 0026772937 scopus 로고
    • Molecular interactions in myosin assembly. Role of the 28-residue charge repeat in the rod
    • Atkinson SJ, Stewart M (1992) Molecular interactions in myosin assembly. Role of the 28-residue charge repeat in the rod. J Mol Biol 226:7-13.
    • (1992) J Mol Biol , vol.226 , pp. 7-13
    • Atkinson, S.J.1    Stewart, M.2
  • 8
    • 33646009721 scopus 로고    scopus 로고
    • Structure and function of myosin filaments
    • Craig R, Woodhead JL (2006) Structure and function of myosin filaments. Curr Opin Struct Biol 16:204-212.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 204-212
    • Craig, R.1    Woodhead, J.L.2
  • 9
    • 0021067370 scopus 로고
    • The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin
    • Nyitray L, et al. (1983) The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin. J Biol Chem 258:13213-13220.
    • (1983) J Biol Chem , vol.258 , pp. 13213-13220
    • Nyitray, L.1
  • 10
    • 0022544420 scopus 로고
    • Solubility-determining domain of smooth muscle myosin rod
    • Cross RA, Vandekerckhove J (1986) Solubility-determining domain of smooth muscle myosin rod. FEBS letters 200:355-360.
    • (1986) FEBS letters , vol.200 , pp. 355-360
    • Cross, R.A.1    Vandekerckhove, J.2
  • 11
    • 0025138386 scopus 로고
    • Expression of Dictyostelium myosin tail segments in Escherichia coli: Domains required for assembly and phosphorylation
    • O'Halloran TJ, Ravid S, Spudich JA (1990) Expression of Dictyostelium myosin tail segments in Escherichia coli: Domains required for assembly and phosphorylation. J Cell Biol 110:63-70.
    • (1990) J Cell Biol , vol.110 , pp. 63-70
    • O'Halloran, T.J.1    Ravid, S.2    Spudich, J.A.3
  • 12
    • 0025642376 scopus 로고
    • Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions
    • Sinard JH, Rimm DL, Pollard TD (1990) Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. J Cell Biol 111:2417-2426.
    • (1990) J Cell Biol , vol.111 , pp. 2417-2426
    • Sinard, J.H.1    Rimm, D.L.2    Pollard, T.D.3
  • 13
    • 0030071619 scopus 로고    scopus 로고
    • Sequences in the myosin II tail required for selfassociation
    • Shoffner JD, De Lozanne A (1996) Sequences in the myosin II tail required for selfassociation. Biochem Bioph Res Co 218:860-864.
    • (1996) Biochem Bioph Res Co , vol.218 , pp. 860-864
    • Shoffner, J.D.1    De Lozanne, A.2
  • 14
    • 0031581843 scopus 로고    scopus 로고
    • A 29 residue region of the sarcomeric myosin rod is necessary for filament formation
    • Sohn RL, et al. (1997) A 29 residue region of the sarcomeric myosin rod is necessary for filament formation. J Mol Biol 266:317-330.
    • (1997) J Mol Biol , vol.266 , pp. 317-330
    • Sohn, R.L.1
  • 15
    • 0031692830 scopus 로고    scopus 로고
    • A conserved C-terminal assembly region in paramyosin and myosin rods
    • Cohen C, Parry DA (1998) A conserved C-terminal assembly region in paramyosin and myosin rods. J Struct Biol 122:180-187.
    • (1998) J Struct Biol , vol.122 , pp. 180-187
    • Cohen, C.1    Parry, D.A.2
  • 16
    • 38049156168 scopus 로고    scopus 로고
    • Filament-dependent and -independent localization modes of Drosophila non-muscle myosin II
    • Liu SL, Fewkes N, Ricketson D, Penkert RR, Prehoda KE (2008) Filament-dependent and -independent localization modes of Drosophila non-muscle myosin II. J Biol Chem 283:380-387.
    • (2008) J Biol Chem , vol.283 , pp. 380-387
    • Liu, S.L.1    Fewkes, N.2    Ricketson, D.3    Penkert, R.R.4    Prehoda, K.E.5
  • 17
    • 0033766762 scopus 로고    scopus 로고
    • A myosin family tree
    • Hodge T, Cope MJ (2000) A myosin family tree. J Cell Sci 113:3353-3354.
    • (2000) J Cell Sci , vol.113 , pp. 3353-3354
    • Hodge, T.1    Cope, M.J.2
  • 19
    • 11844249906 scopus 로고    scopus 로고
    • Critical regions for assembly of vertebrate nonmuscle myosin II
    • Nakasawa T, et al. (2005) Critical regions for assembly of vertebrate nonmuscle myosin II. Biochemistry 44:174-183.
    • (2005) Biochemistry , vol.44 , pp. 174-183
    • Nakasawa, T.1
  • 20
    • 26244466046 scopus 로고    scopus 로고
    • Skip residues and charge interactions in myosin II coiled-coils: Implications for molecular packing
    • Straussman R, Squire JM, Ben-Ya'acov A, Ravid S (2005) Skip residues and charge interactions in myosin II coiled-coils: Implications for molecular packing. J Mol Biol 353:613-628.
    • (2005) J Mol Biol , vol.353 , pp. 613-628
    • Straussman, R.1    Squire, J.M.2    Ben-Ya'acov, A.3    Ravid, S.4
  • 21
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • Burkhard P, Kammerer RA, Steinmetz MO, Bourenkov GP, Aebi U (2000) The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure 8:223-230.
    • (2000) Structure , vol.8 , pp. 223-230
    • Burkhard, P.1    Kammerer, R.A.2    Steinmetz, M.O.3    Bourenkov, G.P.4    Aebi, U.5
  • 23
    • 0016826285 scopus 로고
    • Human platelet myosin. II. In vitro assembly and structure of myosin filaments
    • Niederman R, Pollard TD (1975) Human platelet myosin. II. In vitro assembly and structure of myosin filaments. J Cell Biol 67:72-92.
    • (1975) J Cell Biol , vol.67 , pp. 72-92
    • Niederman, R.1    Pollard, T.D.2
  • 25
    • 14044278735 scopus 로고    scopus 로고
    • Dictyostelium myosin bipolar thick filament formation: Importance of charge and specific domains of the myosin rod
    • Hostetter D, et al. (2004) Dictyostelium myosin bipolar thick filament formation: Importance of charge and specific domains of the myosin rod. PLoS Biol 2:e356.
    • (2004) PLoS Biol , vol.2
    • Hostetter, D.1
  • 26
    • 24144484776 scopus 로고    scopus 로고
    • Atomic model of a myosin filament in the relaxed state
    • Woodhead JL, et al. (2005) Atomic model of a myosin filament in the relaxed state. Nature 436:1195-1199.
    • (2005) Nature , vol.436 , pp. 1195-1199
    • Woodhead, J.L.1
  • 27
    • 40649098633 scopus 로고    scopus 로고
    • Three-dimensional structure of vertebrate cardiac muscle myosin filaments
    • Zoghbi ME, Woodhead JL, Moss RL, Craig R (2008) Three-dimensional structure of vertebrate cardiac muscle myosin filaments. Proc Natl Acad Sci USA 105:2386-2390.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 2386-2390
    • Zoghbi, M.E.1    Woodhead, J.L.2    Moss, R.L.3    Craig, R.4
  • 28
    • 0021399103 scopus 로고
    • Electron microscopic studies on myosin molecules from chicken gizzard muscle III. Myosin dimers
    • Onishi H, Wakabayashi T (1984) Electron microscopic studies on myosin molecules from chicken gizzard muscle III. Myosin dimers. J Biochem 95:903-905.
    • (1984) J Biochem , vol.95 , pp. 903-905
    • Onishi, H.1    Wakabayashi, T.2
  • 29
    • 0021250602 scopus 로고
    • Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength
    • Trybus KM, Lowey S (1984) Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength. J Biol Chem 259:8564-8571.
    • (1984) J Biol Chem , vol.259 , pp. 8564-8571
    • Trybus, K.M.1    Lowey, S.2
  • 30
    • 0023604845 scopus 로고
    • Assembly of smooth muscle myosin minifilaments: Effects of phosphorylation and nucleotide binding
    • Trybus KM, Lowey S (1987) Assembly of smooth muscle myosin minifilaments: Effects of phosphorylation and nucleotide binding. J Cell Biol 105:3007-3019.
    • (1987) J Cell Biol , vol.105 , pp. 3007-3019
    • Trybus, K.M.1    Lowey, S.2
  • 31
    • 0024422071 scopus 로고
    • Brain myosin assembly: Characterization of aggregation-competent fragments by antibodies
    • Barylko B, Zurek B, Jockusch BM (1989) Brain myosin assembly: Characterization of aggregation-competent fragments by antibodies. Eur J Cell Biol 50:41-47.
    • (1989) Eur J Cell Biol , vol.50 , pp. 41-47
    • Barylko, B.1    Zurek, B.2    Jockusch, B.M.3
  • 32
    • 0026011489 scopus 로고
    • A nucleation-elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin
    • Cross RA, Geeves MA, Kendrick-Jones J (1991) A nucleation-elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin. EMBO J 10:747-756.
    • (1991) EMBO J , vol.10 , pp. 747-756
    • Cross, R.A.1    Geeves, M.A.2    Kendrick-Jones, J.3
  • 33
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A (1996) Coiled coils: New structures and new functions. Trends Biochem Sci 21:375-382.
    • (1996) Trends Biochem Sci , vol.21 , pp. 375-382
    • Lupas, A.1
  • 34
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard P, Stetefeld J, Strelkov SV (2001) Coiled coils: A highly versatile protein folding motif. Trends Cell Biol 11:82-88.
    • (2001) Trends Cell Biol , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 35
    • 0019887723 scopus 로고
    • The structure of spindle-shaped paracrystals of light meromyosin
    • Bennett PM (1981) The structure of spindle-shaped paracrystals of light meromyosin. J Mol Biol 146:201-221.
    • (1981) J Mol Biol , vol.146 , pp. 201-221
    • Bennett, P.M.1
  • 36
    • 0017756673 scopus 로고
    • Light meromyosin paracrystal formation
    • Chowrashi PK, Pepe FA (1977) Light meromyosin paracrystal formation. J Cell Biol 74:136-152.
    • (1977) J Cell Biol , vol.74 , pp. 136-152
    • Chowrashi, P.K.1    Pepe, F.A.2
  • 37
    • 0035957287 scopus 로고    scopus 로고
    • Protein kinase C phosphorylates nonmuscle myosin-II heavy chain from Drosophila but regulation of myosin function by this enzyme is not required for viability in flies
    • Su Z, Kiehart DP (2001) Protein kinase C phosphorylates nonmuscle myosin-II heavy chain from Drosophila but regulation of myosin function by this enzyme is not required for viability in flies. Biochemistry 40:3606-3614.
    • (2001) Biochemistry , vol.40 , pp. 3606-3614
    • Su, Z.1    Kiehart, D.P.2
  • 38
    • 1642276423 scopus 로고    scopus 로고
    • Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition
    • Peterson FC, Penkert RR, Volkman BF, Prehoda KE (2004) Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Mol Cell 13:665-676.
    • (2004) Mol Cell , vol.13 , pp. 665-676
    • Peterson, F.C.1    Penkert, R.R.2    Volkman, B.F.3    Prehoda, K.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.