메뉴 건너뛰기




Volumn 87, Issue 8-9, 2008, Pages 709-720

Tropomyosin isoforms define distinct microfilament populations with different drug susceptibility

Author keywords

Actin; Cytochalasin; Latrunculin; siRNA; Tropomyosin

Indexed keywords

ACTIN; ALPHA TROPOMYOSIN; BETA ACTIN; BETA TROPOMYOSIN; CYTOCHALASIN D; GAMMA TROPOMYOSIN; ISOPROTEIN; LATRUNCULIN A; SMALL INTERFERING RNA; TROPOMYOSIN; TROPOMYOSIN 3; TROPOMYOSIN 5;

EID: 49249092510     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2008.03.004     Document Type: Article
Times cited : (32)

References (54)
  • 2
    • 33745353061 scopus 로고    scopus 로고
    • Effects of acrylamide, latrunculin, and nocodazole on intracellular transport and cytoskeletal organization in melanophores
    • Aspengren S., Wielbass L., and Wallin M. Effects of acrylamide, latrunculin, and nocodazole on intracellular transport and cytoskeletal organization in melanophores. Cell Motil. Cytoskeleton 63 (2006) 423-436
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 423-436
    • Aspengren, S.1    Wielbass, L.2    Wallin, M.3
  • 3
    • 0028359143 scopus 로고
    • Identification of novel alternatively spliced isoforms of the tropomyosin-encoding gene, TMnm, in the rat cochlea
    • Beisel K.W., and Kennedy J.E. Identification of novel alternatively spliced isoforms of the tropomyosin-encoding gene, TMnm, in the rat cochlea. Gene 143 (1994) 251-256
    • (1994) Gene , vol.143 , pp. 251-256
    • Beisel, K.W.1    Kennedy, J.E.2
  • 4
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein B.W., and Bamburg J.R. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 2 (1982) 1-8
    • (1982) Cell Motil. , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 5
    • 0022646342 scopus 로고
    • Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament
    • Bonder E.M., and Mooseker M.S. Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament. J. Cell Biol. 102 (1986) 282-288
    • (1986) J. Cell Biol. , vol.102 , pp. 282-288
    • Bonder, E.M.1    Mooseker, M.S.2
  • 6
    • 0025613855 scopus 로고
    • Tropomyosin prevents depolymerization of actin filaments from the pointed end
    • Broschat K.O. Tropomyosin prevents depolymerization of actin filaments from the pointed end. J. Biol. Chem. 265 (1990) 21323-21329
    • (1990) J. Biol. Chem. , vol.265 , pp. 21323-21329
    • Broschat, K.O.1
  • 7
    • 0022930024 scopus 로고
    • Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties
    • Broschat K.O., and Burgess D.R. Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties. J. Biol. Chem. 261 (1986) 13350-13359
    • (1986) J. Biol. Chem. , vol.261 , pp. 13350-13359
    • Broschat, K.O.1    Burgess, D.R.2
  • 8
    • 0024427604 scopus 로고
    • Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization
    • Broschat K.O., Weber A., and Burgess D.R. Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization. Biochemistry 28 (1989) 8501-8506
    • (1989) Biochemistry , vol.28 , pp. 8501-8506
    • Broschat, K.O.1    Weber, A.2    Burgess, D.R.3
  • 9
    • 0018611857 scopus 로고
    • Cytochalasin inhibits the rate of elongation of actin filament fragments
    • Brown S.S., and Spudich J.A. Cytochalasin inhibits the rate of elongation of actin filament fragments. J. Cell Biol. 83 (1979) 657-662
    • (1979) J. Cell Biol. , vol.83 , pp. 657-662
    • Brown, S.S.1    Spudich, J.A.2
  • 10
    • 0019404945 scopus 로고
    • Mechanism of action of cytochalasin: evidence that it binds to actin filament ends
    • Brown S.S., and Spudich J.A. Mechanism of action of cytochalasin: evidence that it binds to actin filament ends. J. Cell Biol. 88 (1981) 487-491
    • (1981) J. Cell Biol. , vol.88 , pp. 487-491
    • Brown, S.S.1    Spudich, J.A.2
  • 12
    • 0035371460 scopus 로고    scopus 로고
    • Multiple combinations of alternatively spliced exons in rat tropomyosin-alpha gene mRNA: evidence for 20 new isoforms in adult tissues and cultured cells
    • Cooley B.C., and Bergtrom G. Multiple combinations of alternatively spliced exons in rat tropomyosin-alpha gene mRNA: evidence for 20 new isoforms in adult tissues and cultured cells. Arch. Biochem. Biophys. 390 (2001) 71-77
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 71-77
    • Cooley, B.C.1    Bergtrom, G.2
  • 13
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper J.A. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105 (1987) 1473-1478
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 14
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: tropomyosin provides stability
    • Cooper J.A. Actin dynamics: tropomyosin provides stability. Curr. Biol. 12 (2002) R523-R525
    • (2002) Curr. Biol. , vol.12
    • Cooper, J.A.1
  • 15
    • 0032541174 scopus 로고    scopus 로고
    • Splicing of two internal and four carboxyl-terminal alternative exons in nonmuscle tropomyosin 5 pre-mRNA is independently regulated during development
    • Dufour C., Weinberger R.P., Schevzov G., Jeffrey P.L., and Gunning P. Splicing of two internal and four carboxyl-terminal alternative exons in nonmuscle tropomyosin 5 pre-mRNA is independently regulated during development. J. Biol. Chem. 273 (1998) 18547-18555
    • (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
  • 16
    • 0037473111 scopus 로고    scopus 로고
    • Establishment of latrunculin-A resistance in HeLa cells by expression of R183A D184A mutant beta-actin
    • Fujita M., Ichinose S., Kiyono T., Tsurumi T., and Omori A. Establishment of latrunculin-A resistance in HeLa cells by expression of R183A D184A mutant beta-actin. Oncogene 22 (2003) 627-631
    • (2003) Oncogene , vol.22 , pp. 627-631
    • Fujita, M.1    Ichinose, S.2    Kiyono, T.3    Tsurumi, T.4    Omori, A.5
  • 17
    • 0642286487 scopus 로고    scopus 로고
    • The actin cytoskeleton as a therapeutic target: state of the art and future directions
    • Giganti A., and Friederich E. The actin cytoskeleton as a therapeutic target: state of the art and future directions. Prog. Cell Cycle Res. 5 (2003) 511-525
    • (2003) Prog. Cell Cycle Res. , vol.5 , pp. 511-525
    • Giganti, A.1    Friederich, E.2
  • 18
    • 0023007962 scopus 로고
    • Actin polymerization. The mechanism of action of cytochalasin D
    • Goddette D.W., and Frieden C. Actin polymerization. The mechanism of action of cytochalasin D. J. Biol. Chem. 261 (1986) 15974-15980
    • (1986) J. Biol. Chem. , vol.261 , pp. 15974-15980
    • Goddette, D.W.1    Frieden, C.2
  • 19
    • 0025887613 scopus 로고
    • Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters
    • Goodwin L.O., Lees-Miller J.P., Leonard M.A., Cheley S.B., and Helfman D.M. Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters. J. Biol. Chem. 266 (1991) 8408-8415
    • (1991) J. Biol. Chem. , vol.266 , pp. 8408-8415
    • Goodwin, L.O.1    Lees-Miller, J.P.2    Leonard, M.A.3    Cheley, S.B.4    Helfman, D.M.5
  • 21
    • 0030947148 scopus 로고    scopus 로고
    • Actin and tropomyosin isoforms in morphogenesis
    • Gunning P., Weinberger R., and Jeffrey P. Actin and tropomyosin isoforms in morphogenesis. Anat. Embryol. 195 (1997) 311-315
    • (1997) Anat. Embryol. , vol.195 , pp. 311-315
    • Gunning, P.1    Weinberger, R.2    Jeffrey, P.3
  • 22
    • 0032211379 scopus 로고    scopus 로고
    • Creating intracellular structural domains: spatial segregation of actin and tropomyosin isoforms in neurons
    • Gunning P., Hardeman E., Jeffrey P., and Weinberger R. Creating intracellular structural domains: spatial segregation of actin and tropomyosin isoforms in neurons. Bioessays 20 (1998) 892-900
    • (1998) Bioessays , vol.20 , pp. 892-900
    • Gunning, P.1    Hardeman, E.2    Jeffrey, P.3    Weinberger, R.4
  • 24
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: divining rods for actin cytoskeleton function
    • Gunning P.W., Schevzov G., Kee A.J., and Hardeman E.C. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol. 15 (2005) 333-341
    • (2005) Trends Cell Biol. , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 25
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning P., O'Neill G., and Herdeman E. Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol. Rev. 88 (2008) 1-35
    • (2008) Physiol. Rev. , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Herdeman, E.3
  • 26
    • 0031841942 scopus 로고    scopus 로고
    • Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein
    • Hannan A.J., Gunning P., Jefferey P.L., and Weinberger R.P. Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein. Mol. Cell. Neurosci. 11 (1998) 289-304
    • (1998) Mol. Cell. Neurosci. , vol.11 , pp. 289-304
    • Hannan, A.J.1    Gunning, P.2    Jefferey, P.L.3    Weinberger, R.P.4
  • 28
    • 0024234768 scopus 로고
    • Tropomyosin inhibits the rate of actin polymerization by stabilizing actin filaments
    • Hitchcock-DeGregori S.E., Sampath P., and Pollard T.D. Tropomyosin inhibits the rate of actin polymerization by stabilizing actin filaments. Biochemistry 27 (1988) 9182-9185
    • (1988) Biochemistry , vol.27 , pp. 9182-9185
    • Hitchcock-DeGregori, S.E.1    Sampath, P.2    Pollard, T.D.3
  • 29
    • 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., and 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. 264 (1989) 7490-7497
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 31
    • 0025247677 scopus 로고
    • Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing
    • Lees-Miller J.P., Goodwin L.O., and Helfman D.M. Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing. Mol. Cell Biol. 10 (1990) 1729-1742
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1729-1742
    • Lees-Miller, J.P.1    Goodwin, L.O.2    Helfman, D.M.3
  • 32
    • 0018830967 scopus 로고
    • Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation
    • Lin D.C., Tobin K.D., Grumet M., and Lin S. Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. J. Cell Biol. 84 (1980) 455-460
    • (1980) J. Cell Biol. , vol.84 , pp. 455-460
    • Lin, D.C.1    Tobin, K.D.2    Grumet, M.3    Lin, S.4
  • 33
    • 0022379564 scopus 로고
    • Purification and characterization of multiple isoforms of tropomyosin from rat cultured cells
    • Matsumura F., and Yamashiro-Matsumura S. Purification and characterization of multiple isoforms of tropomyosin from rat cultured cells. J. Biol. Chem. 260 (1985) 13851-13859
    • (1985) J. Biol. Chem. , vol.260 , pp. 13851-13859
    • Matsumura, F.1    Yamashiro-Matsumura, S.2
  • 34
    • 0032456618 scopus 로고    scopus 로고
    • beta-Actin is confined to structures having high capacity of remodelling in developing and adult rat cerebellum
    • Micheva K.D., Vallee A., Beaulieu C., Herman I.M., and Leclerc N. beta-Actin is confined to structures having high capacity of remodelling in developing and adult rat cerebellum. Eur. J. Neurosci. 10 (1998) 3785-3798
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 3785-3798
    • Micheva, K.D.1    Vallee, A.2    Beaulieu, C.3    Herman, I.M.4    Leclerc, N.5
  • 35
    • 0030935783 scopus 로고    scopus 로고
    • Differential regulation of actin depolymerizing factor and cofilin in response to alterations in the actin monomer pool
    • Minamide L.S., Painter W.B., Schevzov G., Gunning P., and Bamburg J.R. Differential regulation of actin depolymerizing factor and cofilin in response to alterations in the actin monomer pool. J. Biol. Chem. 272 (1997) 8303-8309
    • (1997) J. Biol. Chem. , vol.272 , pp. 8303-8309
    • Minamide, L.S.1    Painter, W.B.2    Schevzov, G.3    Gunning, P.4    Bamburg, J.R.5
  • 36
    • 0036798347 scopus 로고    scopus 로고
    • Latrunculin and cytochalasin decrease chondrocyte matrix retention
    • Nofal G.A., and Knudson C.B. Latrunculin and cytochalasin decrease chondrocyte matrix retention. J. Histochem. Cytochem. 50 (2002) 1313-1324
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 1313-1324
    • Nofal, G.A.1    Knudson, C.B.2
  • 37
    • 0027367331 scopus 로고
    • In vitro functional characterization of bacterially expressed human fibroblast tropomyosin isoforms and their chimeric mutants
    • Novy R.E., Sellers J.R., Liu L.F., and Lin J.J. In vitro functional characterization of bacterially expressed human fibroblast tropomyosin isoforms and their chimeric mutants. Cell Motil. Cytoskeleton 26 (1993) 248-261
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 248-261
    • Novy, R.E.1    Sellers, J.R.2    Liu, L.F.3    Lin, J.J.4
  • 38
    • 37249019968 scopus 로고    scopus 로고
    • Tropomyosins as interpreters of the signalling environment to regulate the local cytoskeleton
    • O'Neill G.M., Stehn J., and Gunning P.W. Tropomyosins as interpreters of the signalling environment to regulate the local cytoskeleton. Semin. Cancer Biol. 18 (2008) 35-44
    • (2008) Semin. Cancer Biol. , vol.18 , pp. 35-44
    • O'Neill, G.M.1    Stehn, J.2    Gunning, P.W.3
  • 39
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono S., and Ono K. Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J. Cell Biol. 156 (2002) 1065-1076
    • (2002) J. Cell Biol. , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 40
    • 1542674372 scopus 로고    scopus 로고
    • B35 neuroblastoma cells: an easily transfected, cultured cell model of central nervous system neurons
    • Otey C.A., Boukhelifa M., and Maness P. B35 neuroblastoma cells: an easily transfected, cultured cell model of central nervous system neurons. Methods Cell Biol. 71 (2003) 287-304
    • (2003) Methods Cell Biol. , vol.71 , pp. 287-304
    • Otey, C.A.1    Boukhelifa, M.2    Maness, P.3
  • 43
    • 0026713920 scopus 로고
    • In vitro and in vivo characterization of four fibroblast tropomyosins produced in bacteria: TM-2, TM-3, TM-5a, and TM-5b are co-localized in interphase fibroblasts
    • Pittenger M.F., and Helfman D.M. In vitro and in vivo characterization of four fibroblast tropomyosins produced in bacteria: TM-2, TM-3, TM-5a, and TM-5b are co-localized in interphase fibroblasts. J. Cell Biol. 118 (1992) 841-858
    • (1992) J. Cell Biol. , vol.118 , pp. 841-858
    • Pittenger, M.F.1    Helfman, D.M.2
  • 44
    • 0031425531 scopus 로고    scopus 로고
    • The 3′-end of the human beta-actin gene enhances activity of the beta-actin expression vector system: construction of improved vectors
    • Qin H., and Gunning P. The 3′-end of the human beta-actin gene enhances activity of the beta-actin expression vector system: construction of improved vectors. J. Biochem. Biophys. Methods 36 (1997) 63-72
    • (1997) J. Biochem. Biophys. Methods , vol.36 , pp. 63-72
    • Qin, H.1    Gunning, P.2
  • 45
    • 0025457288 scopus 로고
    • The functional importance of multiple actin isoforms
    • Rubenstein P.A. The functional importance of multiple actin isoforms. Bioessays 12 (1990) 309-315
    • (1990) Bioessays , vol.12 , pp. 309-315
    • Rubenstein, P.A.1
  • 46
    • 0027262207 scopus 로고
    • Differential regulation of tropomyosin isoform organization and gene expression in response to altered actin gene expression
    • Schevzov G., Lloyd C., Hailstones D., and Gunning P. Differential regulation of tropomyosin isoform organization and gene expression in response to altered actin gene expression. J. Cell Biol. 121 (1993) 811-821
    • (1993) J. Cell Biol. , vol.121 , pp. 811-821
    • Schevzov, G.1    Lloyd, C.2    Hailstones, D.3    Gunning, P.4
  • 50
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector I., Braet F., Shochet N.R., and Bubb M.R. New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc. Res. Tech. 47 (1999) 18-37
    • (1999) Microsc. Res. Tech. , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 52
    • 24344431573 scopus 로고    scopus 로고
    • Differential effects of latrunculin-A on myofibrils in cultures of skeletal muscle cells: insights into mechanisms of myofibrillogenesis
    • Wang J., Sanger J.M., and Sanger J.W. Differential effects of latrunculin-A on myofibrils in cultures of skeletal muscle cells: insights into mechanisms of myofibrillogenesis. Cell Motil. Cytoskeleton 62 (2005) 35-47
    • (2005) Cell Motil. Cytoskeleton , vol.62 , pp. 35-47
    • Wang, J.1    Sanger, J.M.2    Sanger, J.W.3
  • 53
    • 0028926206 scopus 로고
    • Forced expression of chimeric human fibroblast tropomyosin mutants affects cytokinesis
    • Warren K.S., Lin J.L., McDermott J.P., and Lin J.J. Forced expression of chimeric human fibroblast tropomyosin mutants affects cytokinesis. J. Cell Biol. 129 (1995) 697-708
    • (1995) J. Cell Biol. , vol.129 , pp. 697-708
    • Warren, K.S.1    Lin, J.L.2    McDermott, J.P.3    Lin, J.J.4
  • 54
    • 0034623126 scopus 로고    scopus 로고
    • Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A
    • Yarmola E.G., Somasundaram T., Boring T.A., Spector I., and Bubb M.R. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J. Biol. Chem. 275 (2000) 28120-28127
    • (2000) J. Biol. Chem. , vol.275 , pp. 28120-28127
    • Yarmola, E.G.1    Somasundaram, T.2    Boring, T.A.3    Spector, I.4    Bubb, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.