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Volumn 1, Issue 1, 2011, Pages 49-59

Functional identity of the gamma tropomyosin gene: Implications for embryonic development, reproduction and cell viability

Author keywords

Actin; Cytoskeleton; Isoforms; Redundancy; Tropomyosin

Indexed keywords

TROPOMYOSIN;

EID: 84992231763     PISSN: 19490992     EISSN: 1949100X     Source Type: Journal    
DOI: 10.4161/bioa.1.1.15172     Document Type: Article
Times cited : (28)

References (51)
  • 1
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: tropomyosin provides stability
    • Cooper JA. Actin dynamics: tropomyosin provides stability. Curr Biol 2002; 12:523-5.
    • (2002) Curr Biol , vol.12 , pp. 523-525
    • Cooper, J.A.1
  • 2
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller JP, Helfman DM. The molecular basis for tropomyosin isoform diversity. Bioessays 1991; 13:429-37.
    • (1991) Bioessays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 3
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: divining rods for actin cytoskeleton function
    • Gunning PW, Schevzov G, Kee AJ, Hardeman EC. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol 2005; 15:333-41.
    • (2005) Trends Cell Biol , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 5
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosinbased regulation of the actin cytoskeleton in time and space
    • Gunning P, O'Neill G, Hardeman E. Tropomyosinbased regulation of the actin cytoskeleton in time and space. Physiol Rev 2008; 88:1-35.
    • (2008) Physiol Rev , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 6
    • 0029091378 scopus 로고
    • Alternatively spliced exons of the beta tropomyosin gene exhibit different affinities for F-actin and effects with nonmuscle caldesmon
    • Pittenger MF, Kistler A, Helfman DM. Alternatively spliced exons of the beta tropomyosin gene exhibit different affinities for F-actin and effects with nonmuscle caldesmon. J Cell Sci 1995; 108:3253-65.
    • (1995) J Cell Sci , vol.108 , pp. 3253-3265
    • Pittenger, M.F.1    Kistler, A.2    Helfman, D.M.3
  • 7
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein BW, Bamburg JR. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil 1982; 2:1-8.
    • (1982) Cell Motil , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 8
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilindependent actin filament dynamics
    • Ono S, Ono K. Tropomyosin inhibits ADF/cofilindependent actin filament dynamics. J Cell Biol 2002; 156:1065-76.
    • (2002) J Cell Biol , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 9
    • 0024427604 scopus 로고
    • Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization
    • Broschat KO, Weber A, Burgess DR. Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization. Biochemistry 1989; 28:8501-6.
    • (1989) Biochemistry , vol.28 , pp. 8501-8506
    • Broschat, K.O.1    Weber, A.2    Burgess, D.R.3
  • 10
    • 0023139873 scopus 로고
    • Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins
    • Burgess DR, Broschat KO, Hayden JM. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. J Cell Biol 1987; 104:29-40.
    • (1987) J Cell Biol , vol.104 , pp. 29-40
    • Burgess, D.R.1    Broschat, K.O.2    Hayden, J.M.3
  • 11
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • Blanchoin L, Pollard TD, Hitchcock-DeGregori SE. Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin. Curr Biol 2001; 11:1300-4.
    • (2001) Curr Biol , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-DeGregori, S.E.3
  • 12
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin Potentiation of protective ability of tropomyosins by 83 kDa nonmuscle caldesmon
    • Ishikawa R, Yamashiro S, Matsumura F. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83 kDa nonmuscle caldesmon. J Biol Chem 1989; 264:7490-7.
    • (1989) J Biol Chem , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 14
    • 0037343138 scopus 로고    scopus 로고
    • Specification of actin filament function and molecular composition by tropomyosin isoforms
    • Bryce NS, Schevzov G, Ferguson V, Percival JM, Lin JJ, Matsumura F, et al. Specification of actin filament function and molecular composition by tropomyosin isoforms. Mol Biol Cell 2003; 14:1002-16.
    • (2003) Mol Biol Cell , vol.14 , pp. 1002-1016
    • Bryce, N.S.1    Schevzov, G.2    Ferguson, V.3    Percival, J.M.4    Lin, J.J.5    Matsumura, F.6
  • 15
    • 77951975127 scopus 로고    scopus 로고
    • Alternatively spliced N-terminal exons in tropomyosin isoforms do not act as autonomous targeting signals
    • Martin C, Schevzov G, Gunning P. Alternatively spliced N-terminal exons in tropomyosin isoforms do not act as autonomous targeting signals. J Struct Biol 2010; 170:286-93.
    • (2010) J Struct Biol , vol.170 , pp. 286-293
    • Martin, C.1    Schevzov, G.2    Gunning, P.3
  • 17
    • 77956901465 scopus 로고    scopus 로고
    • The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast
    • Coulton AT, East DA, Galinska-Rakoczy A, Lehman W, Mulvihill DP. The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. J Cell Sci 2010; 123:3235-43.
    • (2010) J Cell Sci , vol.123 , pp. 3235-3243
    • Coulton, A.T.1    East, D.A.2    Galinska-Rakoczy, A.3    Lehman, W.4    Mulvihill, D.P.5
  • 18
    • 77957834345 scopus 로고    scopus 로고
    • Differential regulation of unconventional fission yeast myosins via the actin track
    • Clayton JE, Sammons MR, Stark BC, Hodges AR, Lord M. Differential regulation of unconventional fission yeast myosins via the actin track. Curr Biol 2010; 20:1423-31.
    • (2010) Curr Biol , vol.20 , pp. 1423-1431
    • Clayton, J.E.1    Sammons, M.R.2    Stark, B.C.3    Hodges, A.R.4    Lord, M.5
  • 19
    • 77949457529 scopus 로고    scopus 로고
    • Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast
    • Stark BC, Sladewski TE, Pollard LW, Lord M. Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast. Mol Biol Cell 2010; 21:989-1000.
    • (2010) Mol Biol Cell , vol.21 , pp. 989-1000
    • Stark, B.C.1    Sladewski, T.E.2    Pollard, L.W.3    Lord, M.4
  • 20
    • 60849107340 scopus 로고    scopus 로고
    • Tropomyosin gene expression in vivo and in vitro
    • Schevzov G, O'Neill G. Tropomyosin gene expression in vivo and in vitro. Adv Exp Med Biol 2008; 644:43-59.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 43-59
    • Schevzov, G.1    O'Neill, G.2
  • 22
    • 1542374026 scopus 로고    scopus 로고
    • Gamma tropomyosin gene products are required for embryonic development
    • Hook J, Lemckert F, Qin H, Schevzov G, Gunning P. Gamma tropomyosin gene products are required for embryonic development. Mol Cell Biol 2004; 24:2318-23.
    • (2004) Mol Cell Biol , vol.24 , pp. 2318-2323
    • Hook, J.1    Lemckert, F.2    Qin, H.3    Schevzov, G.4    Gunning, P.5
  • 23
    • 77951623501 scopus 로고    scopus 로고
    • Investigations into tropomyosin function using mouse models
    • Jagatheesan G, Rajan S, Wieczorek DF. Investigations into tropomyosin function using mouse models. J Mol Cell Cardiol 2010; 48:893-8.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 893-898
    • Jagatheesan, G.1    Rajan, S.2    Wieczorek, D.F.3
  • 24
    • 0027285642 scopus 로고
    • Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos
    • Muthuchamy M, Pajak L, Howles P, Doetschman T, Wieczorek DF. Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos. Mol Cell Biol 1993; 13:3311.
    • (1993) Mol Cell Biol , vol.13 , pp. 3311
    • Muthuchamy, M.1    Pajak, L.2    Howles, P.3    Doetschman, T.4    Wieczorek, D.F.5
  • 25
    • 0032004877 scopus 로고    scopus 로고
    • Tropomyosin in preimplantation mouse development: identification, expression and organization during cell division and polarization
    • Clayton L, Johnson MH. Tropomyosin in preimplantation mouse development: identification, expression and organization during cell division and polarization. Exp Cell Res 1998; 238:450-64.
    • (1998) Exp Cell Res , vol.238 , pp. 450-464
    • Clayton, L.1    Johnson, M.H.2
  • 26
    • 0032541174 scopus 로고    scopus 로고
    • Splicing of two internal and four carboxylterminal alternative exons in nonmuscle tropomyosin 5 pre-mRNA is independently regulated during development
    • Dufour C, Weinberger RP, Schevzov G, Jeffrey PL, Gunning P. Splicing of two internal and four carboxylterminal alternative exons in nonmuscle tropomyosin 5 pre-mRNA is independently regulated during development. J Biol Chem 1998; 273:18547-55.
    • (1998) J Biol Chem , vol.273 , pp. 18547-18555
    • Dufour, C.1    Weinberger, R.P.2    Schevzov, G.3    Jeffrey, P.L.4    Gunning, P.5
  • 27
    • 5344222725 scopus 로고    scopus 로고
    • Modification of the tropomyosin isoform composition of actin filaments in the brain by deletion of an alternatively spliced exon
    • Vrhovski B, Lemckert F, Gunning P. Modification of the tropomyosin isoform composition of actin filaments in the brain by deletion of an alternatively spliced exon. Neuropharmacology 2004; 47:684-93.
    • (2004) Neuropharmacology , vol.47 , pp. 684-693
    • Vrhovski, B.1    Lemckert, F.2    Gunning, P.3
  • 28
    • 77952009376 scopus 로고    scopus 로고
    • New aspects of tropomyosin-regulated neuritogenesis revealed by the deletion of Tm5NM1 and 2
    • Fath T, Agnes Chan YK, Vrhovski B, Clarke H, Curthoys N, Hook J, et al. New aspects of tropomyosin-regulated neuritogenesis revealed by the deletion of Tm5NM1 and 2. Eur J Cell Biol 2010; 89:489-98.
    • (2010) Eur J Cell Biol , vol.89 , pp. 489-498
    • Fath, T.1    Agnes Chan, Y.K.2    Vrhovski, B.3    Clarke, H.4    Curthoys, N.5    Hook, J.6
  • 29
    • 0025817568 scopus 로고
    • Coordination of skeletal muscle gene expression occurs late in mammalian development
    • Sutherland CJ, Elsom VL, Gordon ML, Dunwoodie SL, Hardeman EC. Coordination of skeletal muscle gene expression occurs late in mammalian development. Dev Biol 1991; 146:167-78.
    • (1991) Dev Biol , vol.146 , pp. 167-178
    • Sutherland, C.J.1    Elsom, V.L.2    Gordon, M.L.3    Dunwoodie, S.L.4    Hardeman, E.C.5
  • 30
    • 34548860663 scopus 로고    scopus 로고
    • Shb null allele is inherited with a transmission ratio distortion and causes reduced viability in utero
    • Kriz V, Mares J, Wentzel P, Funa NS, Calounova G, Zhang XQ, et al. Shb null allele is inherited with a transmission ratio distortion and causes reduced viability in utero. Dev Dyn 2007; 236:2485-92.
    • (2007) Dev Dyn , vol.236 , pp. 2485-2492
    • Kriz, V.1    Mares, J.2    Wentzel, P.3    Funa, N.S.4    Calounova, G.5    Zhang, X.Q.6
  • 31
  • 32
    • 0022035158 scopus 로고
    • Determinants of mating success in the golden hamster (Mesocricetus auratus): I Male capacity
    • Huck UW, Lisk RD. Determinants of mating success in the golden hamster (Mesocricetus auratus): I. Male capacity. J Comp Psychol 1985; 99:98-107.
    • (1985) J Comp Psychol , vol.99 , pp. 98-107
    • Huck, U.W.1    Lisk, R.D.2
  • 33
    • 0016717952 scopus 로고
    • Heterospermic insemination and its effect on the offspring ratio in rats
    • Sharma OP, Hays RL. Heterospermic insemination and its effect on the offspring ratio in rats. J Reprod Fertil 1975; 45:533-5.
    • (1975) J Reprod Fertil , vol.45 , pp. 533-535
    • Sharma, O.P.1    Hays, R.L.2
  • 34
    • 0017059017 scopus 로고
    • Strain differences in the in vitro fertilizing capacity of mouse spermatozoa as tested in various media
    • Parkening TA, Chang MC. Strain differences in the in vitro fertilizing capacity of mouse spermatozoa as tested in various media. Biol Reprod 1976; 15:647-53.
    • (1976) Biol Reprod , vol.15 , pp. 647-653
    • Parkening, T.A.1    Chang, M.C.2
  • 35
    • 0023216732 scopus 로고
    • Penetration of mouse eggs at various intervals after insemination as influenced by concentration of sperm and strain of male
    • Robl JM, Dziuk PJ. Penetration of mouse eggs at various intervals after insemination as influenced by concentration of sperm and strain of male. J Exp Zool 1987; 242:181-7.
    • (1987) J Exp Zool , vol.242 , pp. 181-187
    • Robl, J.M.1    Dziuk, P.J.2
  • 36
    • 0026772201 scopus 로고
    • Localization of actin, alpha-actinin and tropomyosin in bovine spermatozoa and epididymal epithelium
    • Yagi A, Paranko J. Localization of actin, alpha-actinin and tropomyosin in bovine spermatozoa and epididymal epithelium. Anat Rec 1992; 233:61-74.
    • (1992) Anat Rec , vol.233 , pp. 61-74
    • Yagi, A.1    Paranko, J.2
  • 37
    • 33846439765 scopus 로고    scopus 로고
    • F-actin involvement in guinea pig sperm motility
    • Azamar Y, Uribe S, Mujica A. F-actin involvement in guinea pig sperm motility. Mol Reprod Dev 2007; 74:312-20.
    • (2007) Mol Reprod Dev , vol.74 , pp. 312-320
    • Azamar, Y.1    Uribe, S.2    Mujica, A.3
  • 38
    • 36649020854 scopus 로고    scopus 로고
    • The macaque sperm actin cytoskeleton reorganizes in response to osmotic stress and contributes to morphological defects and decreased motility
    • Correa LM, Thomas A, Meyers SA. The macaque sperm actin cytoskeleton reorganizes in response to osmotic stress and contributes to morphological defects and decreased motility. Biol Reprod 2007; 77:942-53.
    • (2007) Biol Reprod , vol.77 , pp. 942-953
    • Correa, L.M.1    Thomas, A.2    Meyers, S.A.3
  • 39
    • 0037369769 scopus 로고    scopus 로고
    • Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction
    • Brener E, Rubinstein S, Cohen G, Shternall K, Rivlin J, Breitbart H. Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction. Biol Reprod 2003; 68:837-45.
    • (2003) Biol Reprod , vol.68 , pp. 837-845
    • Brener, E.1    Rubinstein, S.2    Cohen, G.3    Shternall, K.4    Rivlin, J.5    Breitbart, H.6
  • 40
    • 22544446435 scopus 로고    scopus 로고
    • Cytoskeleton localization in the sperm head prior to fertilization
    • Dvorakova K, Moore HD, Sebkova N, Palecek J. Cytoskeleton localization in the sperm head prior to fertilization. Reproduction 2005; 130:61-9.
    • (2005) Reproduction , vol.130 , pp. 61-69
    • Dvorakova, K.1    Moore, H.D.2    Sebkova, N.3    Palecek, J.4
  • 41
    • 0036150326 scopus 로고    scopus 로고
    • An anti-actin monoclonal antibody inhibits the zona pellucida-induced acrosome reaction and hyperactivated motility of human sperm
    • Liu DY, Martic M, Clarke GN, Grkovic I, Garrett C, Dunlop ME, et al. An anti-actin monoclonal antibody inhibits the zona pellucida-induced acrosome reaction and hyperactivated motility of human sperm. Mol Hum Reprod 2002; 8:37-47.
    • (2002) Mol Hum Reprod , vol.8 , pp. 37-47
    • Liu, D.Y.1    Martic, M.2    Clarke, G.N.3    Grkovic, I.4    Garrett, C.5    Dunlop, M.E.6
  • 42
    • 78650039249 scopus 로고    scopus 로고
    • The role and regulation of sperm gelsolin prior to fertilization
    • DOI:10.1074/jbcM110 170951
    • Finkelstein M, Etkovitz N, Breitbart H. The role and regulation of sperm gelsolin prior to fertilization. J Biol Chem; DOI:10.1074/jbcM110 170951.
    • J Biol Chem
    • Finkelstein, M.1    Etkovitz, N.2    Breitbart, H.3
  • 43
    • 77954594769 scopus 로고    scopus 로고
    • Analysis of CAPZA3 localization reveals temporally discrete events during the acrosome reaction
    • Sosnik J, Buffone MG, Visconti PE. Analysis of CAPZA3 localization reveals temporally discrete events during the acrosome reaction. J Cell Physiol 2009; 224:575-80.
    • (2009) J Cell Physiol , vol.224 , pp. 575-580
    • Sosnik, J.1    Buffone, M.G.2    Visconti, P.E.3
  • 44
    • 0029918141 scopus 로고    scopus 로고
    • Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity
    • Dabrowska R, Hinssen H, Galazkiewicz B, Nowak E. Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity. Biochem J 1996; 315:753-9.
    • (1996) Biochem J , vol.315 , pp. 753-759
    • Dabrowska, R.1    Hinssen, H.2    Galazkiewicz, B.3    Nowak, E.4
  • 45
    • 0028954614 scopus 로고
    • Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions
    • Drees B, Brown C, Barrell BG, Bretscher A. Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions. J Cell Biol 1995; 128:383-92.
    • (1995) J Cell Biol , vol.128 , pp. 383-392
    • Drees, B.1    Brown, C.2    Barrell, B.G.3    Bretscher, A.4
  • 46
    • 0025930750 scopus 로고
    • Small differences in Drosophila tropomyosin expression have significant effects on muscle function
    • Tansey T, Schultz JR, Miller RC, Storti RV. Small differences in Drosophila tropomyosin expression have significant effects on muscle function. Mol Cell Biol 1991; 11:6337-42.
    • (1991) Mol Cell Biol , vol.11 , pp. 6337-6342
    • Tansey, T.1    Schultz, J.R.2    Miller, R.C.3    Storti, R.V.4
  • 47
    • 0029844404 scopus 로고    scopus 로고
    • Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants
    • Kreuz AJ, Simcox A, Maughan D. Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants. J Cell Biol 1996; 135:673-87.
    • (1996) J Cell Biol , vol.135 , pp. 673-687
    • Kreuz, A.J.1    Simcox, A.2    Maughan, D.3
  • 48
    • 0029977564 scopus 로고    scopus 로고
    • Lack of Drosophila cytoskeletal tropomyosin affects head morphogenesis and the accumulation of oskar mRNA required for germ cell formation
    • Tetzlaff MT, Jackle H, Pankratz MJ. Lack of Drosophila cytoskeletal tropomyosin affects head morphogenesis and the accumulation of oskar mRNA required for germ cell formation. EMBO J 1996; 15:1247-54.
    • (1996) EMBO J , vol.15 , pp. 1247-1254
    • Tetzlaff, M.T.1    Jackle, H.2    Pankratz, M.J.3
  • 49
    • 0023808937 scopus 로고
    • Differential localization of tropomyosin isoforms in cultured nonmuscle cells
    • Lin JJ, Hegmann TE, Lin JL. Differential localization of tropomyosin isoforms in cultured nonmuscle cells. J Cell Biol 1988; 107:563-72.
    • (1988) J Cell Biol , vol.107 , pp. 563-572
    • Lin, J.J.1    Hegmann, T.E.2    Lin, J.L.3
  • 51
    • 0031841942 scopus 로고    scopus 로고
    • Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein
    • Hannan AJ, Gunning P, Jeffrey PL, Weinberger RP. Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein. Mol Cell Neurosci 1998; 11:289-304.
    • (1998) Mol Cell Neurosci , vol.11 , pp. 289-304
    • Hannan, A.J.1    Gunning, P.2    Jeffrey, P.L.3    Weinberger, R.P.4


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