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Volumn 118, Issue 17, 2005, Pages 3937-3948

Contribution of sequence variation in Drosophila actins to their incorporation into actin-based structures in vivo

Author keywords

Cytoskeleton; Filopodia; Muscle; Oogenesis; Sarcomere

Indexed keywords

ACTIN; DROSOPHILA PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN;

EID: 26244446828     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02517     Document Type: Article
Times cited : (56)

References (58)
  • 1
    • 0028013757 scopus 로고
    • Membrane-actin microfilament connections: An increasing diversity of players related to band 4.1
    • Arpin, M., Algrain, M. and Louvard, D. (1994). Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1. Curr. Opin. Cell Biol. 6, 136-141.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 136-141
    • Arpin, M.1    Algrain, M.2    Louvard, D.3
  • 3
    • 0001568287 scopus 로고
    • The mesoderm and its derivatives
    • (ed. M. Bate and A. Martinez-Arias), Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press
    • Bate, M. (1993). The mesoderm and its derivatives. In The Development of Drosophila Melanogaster (ed. M. Bate and A. Martinez-Arias), pp. 1013-1090. Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press.
    • (1993) The Development of Drosophila Melanogaster , pp. 1013-1090
    • Bate, M.1
  • 4
    • 0035806975 scopus 로고    scopus 로고
    • The receptor tyrosine phosphatase Dlar and integrins organize actin filaments in the Drosophila follicular epithelium
    • Bateman, J., Reddy, R. S., Saito, H. and Van Vactor, D. (2001). The receptor tyrosine phosphatase Dlar and integrins organize actin filaments in the Drosophila follicular epithelium. Curr. Biol. 11, 1317-1327.
    • (2001) Curr. Biol. , vol.11 , pp. 1317-1327
    • Bateman, J.1    Reddy, R.S.2    Saito, H.3    Van Vactor, D.4
  • 5
    • 0024617347 scopus 로고
    • Genetic dissection of Drosophila myofibril formation: Effects of actin and myosin heavy chain null alleles
    • Beall, C. J., Sepanski, M. A. and Fyrberg, E. A. (1989). Genetic dissection of Drosophila myofibril formation: effects of actin and myosin heavy chain null alleles. Genes Dev. 3, 131-140.
    • (1989) Genes Dev. , vol.3 , pp. 131-140
    • Beall, C.J.1    Sepanski, M.A.2    Fyrberg, E.A.3
  • 6
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. H. and Perrimon, N. (1993). Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 7
    • 0032717712 scopus 로고    scopus 로고
    • Substitution of flight muscle-specific actin by human (beta)-cytoplasmic actin in the indirect flight muscle of Drosophila
    • Brault, V., Reedy, M. C., Sauder, U., Kammerer, R. A., Aebi, U. and Schoenenberger, C. (1999a). Substitution of flight muscle-specific actin by human (beta)-cytoplasmic actin in the indirect flight muscle of Drosophila. J. Cell Sci. 112, 3627-3639.
    • (1999) J. Cell Sci. , vol.112 , pp. 3627-3639
    • Brault, V.1    Reedy, M.C.2    Sauder, U.3    Kammerer, R.A.4    Aebi, U.5    Schoenenberger, C.6
  • 8
    • 0032894399 scopus 로고    scopus 로고
    • Differential epitope tagging of actin in transformed Drosophila produces distinct effects on myofibril assembly and function of the indirect flight muscle
    • Brault, V., Sauder, U., Reedy, M. C., Aebi, U. and Schoenenberger, C. A. (1999b). Differential epitope tagging of actin in transformed Drosophila produces distinct effects on myofibril assembly and function of the indirect flight muscle. Mol. Biol. Cell 10, 135-149.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 135-149
    • Brault, V.1    Sauder, U.2    Reedy, M.C.3    Aebi, U.4    Schoenenberger, C.A.5
  • 9
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher, A. (1991). Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7, 337-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 11
    • 0024410410 scopus 로고
    • Functional sorting of actin isoforms in microvascular pericytes
    • DeNofrio, D., Houck, T. C. and Herman, I. M. (1989). Functional sorting of actin isoforms in microvascular pericytes. J. Cell Biol. 109, 191-202.
    • (1989) J. Cell Biol. , vol.109 , pp. 191-202
    • DeNofrio, D.1    Houck, T.C.2    Herman, I.M.3
  • 12
    • 0034627754 scopus 로고    scopus 로고
    • F-actin bundles are derivatives of microvilli: What does this tell us about how bundles might form?
    • DeRosier, D. J. and Tilney, L. G. (2000). F-actin bundles are derivatives of microvilli: What does this tell us about how bundles might form? J. Cell Biol. 148, 1-6.
    • (2000) J. Cell Biol. , vol.148 , pp. 1-6
    • DeRosier, D.J.1    Tilney, L.G.2
  • 13
    • 0025824515 scopus 로고
    • Localization of isoactins in isolated smooth muscle thin filaments by double gold immunolabeling
    • Drew, J. S., Moos, C. and Murphy, R. A. (1991). Localization of isoactins in isolated smooth muscle thin filaments by double gold immunolabeling. Am. J. Physiol. 260, C1332-C1340.
    • (1991) Am. J. Physiol. , vol.260
    • Drew, J.S.1    Moos, C.2    Murphy, R.A.3
  • 14
    • 0020581716 scopus 로고
    • Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner
    • Fyrberg, E. A., Mahaffey, J. W., Bond, B. J. and Davidson, N. (1983). Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Cell 33, 115-123.
    • (1983) Cell , vol.33 , pp. 115-123
    • Fyrberg, E.A.1    Mahaffey, J.W.2    Bond, B.J.3    Davidson, N.4
  • 16
    • 0030814006 scopus 로고    scopus 로고
    • Actin filament cables in Drosophila nurse cells are composed of modules that slide passively past one another during dumping
    • Guild, G. M., Connelly, P. S., Shaw, M. K. and Tilney, L. G. (1997). Actin filament cables in Drosophila nurse cells are composed of modules that slide passively past one another during dumping. J. Cell Biol. 138, 783-797.
    • (1997) J. Cell Biol. , vol.138 , pp. 783-797
    • Guild, G.M.1    Connelly, P.S.2    Shaw, M.K.3    Tilney, L.G.4
  • 17
    • 0027184250 scopus 로고
    • Beta and gamma actin mRNAs are differentially located within myoblasts
    • Hill, M. A. and Gunning, P. (1993). Beta and gamma actin mRNAs are differentially located within myoblasts. J. Cell Biol. 122, 825-832.
    • (1993) J. Cell Biol. , vol.122 , pp. 825-832
    • Hill, M.A.1    Gunning, P.2
  • 18
    • 0028178791 scopus 로고
    • The basic-hetix-loop-helix domain of Drosophila lethal of scute protein is sufficient for proneural function and activates neurogenic genes
    • Hinz, U., Giebel, B. and Campos-Ortega, J. A. (1994). The basic-hetix-loop-helix domain of Drosophila lethal of scute protein is sufficient for proneural function and activates neurogenic genes. Cell 76, 77-87.
    • (1994) Cell , vol.76 , pp. 77-87
    • Hinz, U.1    Giebel, B.2    Campos-Ortega, J.A.3
  • 19
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • Holmes, K. C., Popp, D., Gebhard, W. and Kabsch, W. (1990). Atomic model of the actin filament. Nature 347, 44-49.
    • (1990) Nature , vol.347 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 20
    • 0026058131 scopus 로고
    • Beta actin and its mRNA are localized at the plasma membrane and the regions of moving cytoplasm during the cellular response to injury
    • Hoock, T. C., Newcomb, P. M. and Herman, I. M. (1991). Beta actin and its mRNA are localized at the plasma membrane and the regions of moving cytoplasm during the cellular response to injury. J. Cell Biol. 112, 653-664.
    • (1991) J. Cell Biol. , vol.112 , pp. 653-664
    • Hoock, T.C.1    Newcomb, P.M.2    Herman, I.M.3
  • 21
    • 0001991929 scopus 로고    scopus 로고
    • Recovery of DNA sequences flanking P-element insertions: Inverse PCR and plasmid recue
    • (ed. W. Sullivan, M. Ashburner and R. S. Hawley), Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press
    • Huang, A. M., Rehm, E. J. and Rubin, G. M. (2000). Recovery of DNA sequences flanking P-element insertions: Inverse PCR and plasmid recue. In Drosophila Protocols (ed. W. Sullivan, M. Ashburner and R. S. Hawley), pp. 429-437. Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press.
    • (2000) Drosophila Protocols , pp. 429-437
    • Huang, A.M.1    Rehm, E.J.2    Rubin, G.M.3
  • 23
    • 0036063057 scopus 로고    scopus 로고
    • Dynamic analysis of dorsal closure in Drosophila: From genetics to cell biology
    • Jacinto, A., Woolner, S. and Martin, P. (2002). Dynamic analysis of dorsal closure in Drosophila: from genetics to cell biology. Dev. Cell 3, 9-19.
    • (2002) Dev. Cell , vol.3 , pp. 9-19
    • Jacinto, A.1    Woolner, S.2    Martin, P.3
  • 25
    • 0028027909 scopus 로고
    • Sequences responsible for intracellular localization of beta-actin messenger RNA also affect cell phenotype
    • Kislauskis, E. H., Zhu, X. and Singer, R. H. (1994). Sequences responsible for intracellular localization of beta-actin messenger RNA also affect cell phenotype. J. Cell Biol. 127, 441-451.
    • (1994) J. Cell Biol. , vol.127 , pp. 441-451
    • Kislauskis, E.H.1    Zhu, X.2    Singer, R.H.3
  • 26
    • 0025873299 scopus 로고
    • The role of solation-contraction coupling in regulating stress fiber dynamics in nonmuscle cells
    • Kolega, J., Janson, L. W. and Taylor, D. L. (1991). The role of solation-contraction coupling in regulating stress fiber dynamics in nonmuscle cells. J. Cell Biol. 114, 993-1003.
    • (1991) J. Cell Biol. , vol.114 , pp. 993-1003
    • Kolega, J.1    Janson, L.W.2    Taylor, D.L.3
  • 27
    • 0014989548 scopus 로고
    • The formation of ring canals by cell furrows in Drosophila
    • Mahowald, A. P. (1971). The formation of ring canals by cell furrows in Drosophila. Z Zellforsch. Mikrosk. Anat. 118, 162-167.
    • (1971) Z. Zellforsch. Mikrosk. Anat. , vol.118 , pp. 162-167
    • Mahowald, A.P.1
  • 28
    • 0035842887 scopus 로고    scopus 로고
    • Thin filaments elongate from their pointed ends during myofibril assembly in Drosophila indirect flight muscle
    • Mardahl-Dumesnil, M. and Fowler, V. M. (2001). Thin filaments elongate from their pointed ends during myofibril assembly in Drosophila indirect flight muscle. J. Cell Biol. 155, 1043-1053.
    • (2001) J. Cell Biol. , vol.155 , pp. 1043-1053
    • Mardahl-Dumesnil, M.1    Fowler, V.M.2
  • 29
    • 0021959998 scopus 로고
    • Identical distribution of fluorescently labelled brain and muscle actins in living cardiac fibroblasts and myocytes
    • McKenna, N., Meigs, J. B. and Wang, Y. L. (1985). Identical distribution of fluorescently labelled brain and muscle actins in living cardiac fibroblasts and myocytes. J. Cell Biol. 100, 292-296.
    • (1985) J. Cell Biol. , vol.100 , pp. 292-296
    • McKenna, N.1    Meigs, J.B.2    Wang, Y.L.3
  • 30
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: Pivotal role of the filament barbed end
    • Mejillano, M. R., Kojima, S., Applewhite, D. A., Gertler, F. B., Svitkina, T. M. and Borisy, G. G. (2004). Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118, 363-373.
    • (2004) Cell , vol.118 , pp. 363-373
    • Mejillano, M.R.1    Kojima, S.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5    Borisy, G.G.6
  • 32
    • 0034708341 scopus 로고    scopus 로고
    • Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism
    • Moores, C. A., Keep, N. H. and 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
  • 33
    • 0030909829 scopus 로고    scopus 로고
    • Transfected muscle and non-muscle actins are differentially sorted by cultured smooth muscle and non-muscle cells
    • Mounier, N., Perriard, J. C., Gabbiani, G. and Chaponnier, C. (1997). Transfected muscle and non-muscle actins are differentially sorted by cultured smooth muscle and non-muscle cells. J. Cell Sci. 110, 839-846.
    • (1997) J. Cell Sci. , vol.110 , pp. 839-846
    • Mounier, N.1    Perriard, J.C.2    Gabbiani, G.3    Chaponnier, C.4
  • 34
    • 0034901458 scopus 로고    scopus 로고
    • Expression and function of the Drosophila ACT88F actin isoform is not restricted to the indirect flight muscles
    • Nongthomba, U., Pasalodos-Sanchez, S., Clark, S., Clayton, J. D. and Sparrow, J. C. (2001). Expression and function of the Drosophila ACT88F actin isoform is not restricted to the indirect flight muscles. J. Muscle Res. Cell Motil. 22, 111-119.
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 111-119
    • Nongthomba, U.1    Pasalodos-Sanchez, S.2    Clark, S.3    Clayton, J.D.4    Sparrow, J.C.5
  • 35
    • 2442481067 scopus 로고    scopus 로고
    • Alpha-actinin revisited: A fresh look at an old player
    • Otey, C. A. and Carpen, O. (2004). Alpha-actinin revisited: a fresh look at an old player. Cell Motil. Cytoskeleton 58, 104-111.
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 36
    • 3042710591 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics by actin-monomer-binding proteins
    • Paavilainen, V. O., Bertling, E., Falck, S. and Lappalainen, P. (2004). Regulation of cytoskeletal dynamics by actin-monomer-binding proteins. Trends Cell Biol. 14, 386-394.
    • (2004) Trends Cell Biol. , vol.14 , pp. 386-394
    • Paavilainen, V.O.1    Bertling, E.2    Falck, S.3    Lappalainen, P.4
  • 37
    • 0030782345 scopus 로고    scopus 로고
    • Ectopic activation of torpedo/Egfr, a Drosophila receptor tyrosine kinase, dorsalizes both the eggshell and the embryo
    • Queenan, A. M., Ghabrial, A. and Schupbach, T. (1997). Ectopic activation of torpedo/Egfr, a Drosophila receptor tyrosine kinase, dorsalizes both the eggshell and the embryo. Development 124, 3871-3880.
    • (1997) Development , vol.124 , pp. 3871-3880
    • Queenan, A.M.1    Ghabrial, A.2    Schupbach, T.3
  • 38
    • 0029992508 scopus 로고    scopus 로고
    • Wingless signaling induces nautilus expression in the ventral mesoderm of the Drosophila embryo
    • Ranganayakulu, G., Schulz, R. A. and Olson, E. N. (1996). Wingless signaling induces nautilus expression in the ventral mesoderm of the Drosophila embryo. Dev. Biol. 176, 143-148.
    • (1996) Dev. Biol. , vol.176 , pp. 143-148
    • Ranganayakulu, G.1    Schulz, R.A.2    Olson, E.N.3
  • 39
    • 0027133588 scopus 로고
    • Ultrastructure of developing flight muscle in Drosophila. I. Assembly of myofibrils
    • Reedy, M. C. and Beall, C. (1993a). Ultrastructure of developing flight muscle in Drosophila. I. Assembly of myofibrils. Dev. Biol. 160, 443-465.
    • (1993) Dev. Biol. , vol.160 , pp. 443-465
    • Reedy, M.C.1    Beall, C.2
  • 40
    • 0027133160 scopus 로고
    • Ultrastructure of developing flight muscle in Drosophila. II. Formation of the myotendon junction
    • Reedy, M. C. and Beall, C. (1993b). Ultrastructure of developing flight muscle in Drosophila. II. Formation of the myotendon junction. Dev. Biol. 160, 466-479.
    • (1993) Dev. Biol. , vol.160 , pp. 466-479
    • Reedy, M.C.1    Beall, C.2
  • 41
    • 3543083870 scopus 로고    scopus 로고
    • The co-workers of actin filaments: From cell structures to signals
    • Revenu, C., Athman, R., Robine, S. and Louvard, D. (2004). The co-workers of actin filaments: from cell structures to signals. Nat. Rev. Mol. Cell Biol. 5, 635-646.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 635-646
    • Revenu, C.1    Athman, R.2    Robine, S.3    Louvard, D.4
  • 42
    • 0030969705 scopus 로고    scopus 로고
    • Formation of the Drosophila ovarian ring canal inner rim depends on cheerio
    • Robinson, D. N., Smith-Leiker, T. A., Sokol, N. S., Hudson, A. M. and Cooley, L. (1997). Formation of the Drosophila ovarian ring canal inner rim depends on cheerio. Genetics 145, 1063-1072.
    • (1997) Genetics , vol.145 , pp. 1063-1072
    • Robinson, D.N.1    Smith-Leiker, T.A.2    Sokol, N.S.3    Hudson, A.M.4    Cooley, L.5
  • 43
    • 0141641125 scopus 로고    scopus 로고
    • Maintaining epithelial integrity: A function for gigantic spectraplakin isoforms in adherens junctions
    • Röper, K. and Brown, N. H. (2003). Maintaining epithelial integrity: a function for gigantic spectraplakin isoforms in adherens junctions. J. Cell Biol. 162, 1305-1315.
    • (2003) J. Cell Biol. , vol.162 , pp. 1305-1315
    • Röper, K.1    Brown, N.H.2
  • 44
    • 0031698273 scopus 로고    scopus 로고
    • Gal4 in the Drosophila female germline
    • Rørth, P. (1998). Gal4 in the Drosophila female germline. Mech. Dev. 78, 113-118.
    • (1998) Mech. Dev. , vol.78 , pp. 113-118
    • Rørth, P.1
  • 45
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • Schafer, D. A. (2002). Coupling actin dynamics and membrane dynamics during endocytosis. Curr. Opin. Cell Biol. 14, 76-81.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 76-81
    • Schafer, D.A.1
  • 50
    • 0033523942 scopus 로고    scopus 로고
    • Drosophila filamin encoded by the cheerio locus is a component of ovarian ring canals
    • Sokol, N. S. and Cooley, L. (1999). Drosophila filamin encoded by the cheerio locus is a component of ovarian ring canals. Curr. Biol. 9, 1221-1230.
    • (1999) Curr. Biol. , vol.9 , pp. 1221-1230
    • Sokol, N.S.1    Cooley, L.2
  • 51
    • 0033762550 scopus 로고    scopus 로고
    • Heterogeneous distribution of isoactins in cultured vascular smooth muscle cells does not reflect segregation of contractile and cytoskeletal domains
    • Song, J., Worth, N. F., Rolfe, B. E., Campbell, G. R. and Campbell, J. H. (2000). Heterogeneous distribution of isoactins in cultured vascular smooth muscle cells does not reflect segregation of contractile and cytoskeletal domains. J. Histochem. Cytochem. 48, 1441-1452.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1441-1452
    • Song, J.1    Worth, N.F.2    Rolfe, B.E.3    Campbell, G.R.4    Campbell, J.H.5
  • 54
    • 0032510041 scopus 로고    scopus 로고
    • Regulation of zygotic gene expression in Drosophila primordial germ cells
    • Van Doren, M., Williamson, A. L. and Lehmann, R. (1998). Regulation of zygotic gene expression in Drosophila primordial germ cells. Curr. Biol. 8, 243-246.
    • (1998) Curr. Biol. , vol.8 , pp. 243-246
    • Van Doren, M.1    Williamson, A.L.2    Lehmann, R.3
  • 55
    • 0035140977 scopus 로고    scopus 로고
    • Actin dynamics and cell-cell adhesion in epithelia
    • Vasioukhin, V. and Fuchs, E. (2001). Actin dynamics and cell-cell adhesion in epithelia. Curr. Opin. Cell Biol. 13, 76-84.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 76-84
    • Vasioukhin, V.1    Fuchs, E.2
  • 56
    • 0033052254 scopus 로고    scopus 로고
    • Actin dynamics in lamellipodia of migrating border cells in the Drosophila ovary revealed by a GFP-actin fusion protein
    • Verkhusha, V. V., Tsukita, S. and Oda, H. (1999). Actin dynamics in lamellipodia of migrating border cells in the Drosophila ovary revealed by a GFP-actin fusion protein. FEBS Lett. 445, 395-401.
    • (1999) FEBS Lett. , vol.445 , pp. 395-401
    • Verkhusha, V.V.1    Tsukita, S.2    Oda, H.3
  • 57
    • 0029615379 scopus 로고
    • Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function
    • von Arx, P., Bantle, S., Soldati, T. and Perriard, J. C. (1995). Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function. J. Cell Biol. 131, 1759-1773.
    • (1995) J. Cell Biol. , vol.131 , pp. 1759-1773
    • von Arx, P.1    Bantle, S.2    Soldati, T.3    Perriard, J.C.4
  • 58
    • 0037062406 scopus 로고    scopus 로고
    • One of the two cytoplasmic actin isoforms in Drosophila. is essential
    • Wagner, C. R., Mahowald, A. P. and Miller, K. G. (2002). One of the two cytoplasmic actin isoforms in Drosophila. is essential. Proc. Natl. Acad. Sci. USA 99, 8037-8042.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8037-8042
    • Wagner, C.R.1    Mahowald, A.P.2    Miller, K.G.3


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