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Volumn 158, Issue 7, 2002, Pages 1219-1228

Actin turnover is required to prevent axon retraction driven by endogenous actomyosin contractility

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN; EPHRIN A2; F ACTIN; JASPAMIDE; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0037144812     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200204140     Document Type: Article
Times cited : (115)

References (48)
  • 1
    • 0033625536 scopus 로고    scopus 로고
    • Motor proteins regulate force interactions between microtubules and microfilaments in the axon
    • Ahmad, F.J., J. Hughey, T. Wittmann, A. Hyman, M. Greaser, and P.W. Baas. 2000. Motor proteins regulate force interactions between microtubules and microfilaments in the axon. Nat. Cell Biol. 2:276-280.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 276-280
    • Ahmad, F.J.1    Hughey, J.2    Wittmann, T.3    Hyman, A.4    Greaser, M.5    Baas, P.W.6
  • 3
    • 0027738697 scopus 로고
    • Myosin light chain kinase occurs in bullfrog sympathetic neurons and may modulate voltage-dependent potassium currents
    • Akasu, T., M. Ito, T. Nakano, C.R. Schneider, M.A. Simmons, T. Tanaka, T. Tokimasa, and M. Yoshida. 1993. Myosin light chain kinase occurs in bullfrog sympathetic neurons and may modulate voltage-dependent potassium currents. Neuron. 11:1133-1145.
    • (1993) Neuron , vol.11 , pp. 1133-1145
    • Akasu, T.1    Ito, M.2    Nakano, T.3    Schneider, C.R.4    Simmons, M.A.5    Tanaka, T.6    Tokimasa, T.7    Yoshida, M.8
  • 4
    • 0034649660 scopus 로고    scopus 로고
    • Endocytosis and the development of cell polarity in yeast require a dynamic F-actin cytoskeleton
    • Ayscough, K.R. 2000. Endocytosis and the development of cell polarity in yeast require a dynamic F-actin cytoskeleton. Curr. Biol. 10:1587-1590.
    • (2000) Curr. Biol. , vol.10 , pp. 1587-1590
    • Ayscough, K.R.1
  • 5
    • 0035913909 scopus 로고    scopus 로고
    • Regulating axon branch stability: The role ofpl90 RhoGAP in repressing a retraction signaling pathway
    • Billuart, P., C.G. Winter, A. Maresh, X. Zhao, and L. Luo. 2001. Regulating axon branch stability: the role ofpl90 RhoGAP in repressing a retraction signaling pathway. Cell. 107:195-207.
    • (2001) Cell , vol.107 , pp. 195-207
    • Billuart, P.1    Winter, C.G.2    Maresh, A.3    Zhao, X.4    Luo, L.5
  • 7
    • 0033583284 scopus 로고    scopus 로고
    • The role of local actin instability in axon formation
    • Bradke, F., and C.G. Dotti. 1999. The role of local actin instability in axon formation. Science. 283:1931-1934.
    • (1999) Science , vol.283 , pp. 1931-1934
    • Bradke, F.1    Dotti, C.G.2
  • 8
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-II regulation
    • Bresnick, A.R. 1999. Molecular mechanisms of nonmuscle myosin-II regulation. Curr. Opin. Cell Biol. 11:26-33.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 26-33
    • Bresnick, A.R.1
  • 9
    • 0024496238 scopus 로고
    • The organization of myosin and actin in rapid frozen nerve growth cones
    • Bridgman, P.C., and M.E. Dailey. 1989. The organization of myosin and actin in rapid frozen nerve growth cones. J. Cell Biol. 108:95-109.
    • (1989) J. Cell Biol. , vol.108 , pp. 95-109
    • Bridgman, P.C.1    Dailey, M.E.2
  • 11
    • 0028244823 scopus 로고
    • Jasplakinolide, a cytotoxic natural product, induced actin polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Bubb, M.R., A.M. Senderowicz, E.A. Sausville, K.L. Duncan, and E.D. Korn. 1994. Jasplakinolide, a cytotoxic natural product, induced actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269:14869-14871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14869-14871
    • Bubb, M.R.1    Senderowicz, A.M.2    Sausville, E.A.3    Duncan, K.L.4    Korn, E.D.5
  • 12
    • 0034681423 scopus 로고    scopus 로고
    • Effects ofjasplakinolide on the kinetics ofactin polymerization
    • Bubb, M.R., I. Spector, B.B. Beyer, and K.M. Fosen. 2000. Effects ofjasplakinolide on the kinetics ofactin polymerization. J. Biol. Chem. 275:5163-5170.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 13
    • 0033533744 scopus 로고    scopus 로고
    • Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide
    • Cramer, L.P. 1999. Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide. Curr. Biol. 9:1095-1105.
    • (1999) Curr. Biol. , vol.9 , pp. 1095-1105
    • Cramer, L.P.1
  • 14
    • 0034652197 scopus 로고    scopus 로고
    • Stabilization of growing retinal axons by the combined signaling of nitric oxide and brain-derived neurotrophic factor
    • Ernst, A.F., G. Gallo, P.C. Letourneau, and S.C. McLoon. 2000. Stabilization of growing retinal axons by the combined signaling of nitric oxide and brain-derived neurotrophic factor. J. Neurosci. 20:1458-1469.
    • (2000) J. Neurosci. , vol.20 , pp. 1458-1469
    • Ernst, A.F.1    Gallo, G.2    Letourneau, P.C.3    McLoon, S.C.4
  • 15
    • 0027192866 scopus 로고
    • The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor
    • Fan, J., S.G. Mansfield, T. Redmond, P.R. Gordon-Weeks, and J.A. Raper. 1993. The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor. J. Cell Biol. 121:867-878.
    • (1993) J. Cell Biol. , vol.121 , pp. 867-878
    • Fan, J.1    Mansfield, S.G.2    Redmond, T.3    Gordon-Weeks, P.R.4    Raper, J.A.5
  • 16
    • 0032527591 scopus 로고    scopus 로고
    • Localized sources of neurotrophins initiate axon collateral sprouting
    • Gallo, G., and P.C. Letourneau. 1998. Localized sources of neurotrophins initiate axon collateral sprouting. J. Neurosci. 18:5403-5414.
    • (1998) J. Neurosci. , vol.18 , pp. 5403-5414
    • Gallo, G.1    Letourneau, P.C.2
  • 17
    • 0033562789 scopus 로고    scopus 로고
    • Different contributions of microtubule dynamics and transport to the growth of axons and collateral sprouts
    • Gallo, G., and P.C. Letourneau. 1999. Different contributions of microtubule dynamics and transport to the growth of axons and collateral sprouts. J. Neurosci. 19:3860-3873.
    • (1999) J. Neurosci. , vol.19 , pp. 3860-3873
    • Gallo, G.1    Letourneau, P.C.2
  • 18
    • 0028241496 scopus 로고
    • Mechanical tension as a regulator of axonal development
    • Heidemann, S.R., and R.E. Buxbaum. 1994. Mechanical tension as a regulator of axonal development. Neurotoxicology. 15:95-107.
    • (1994) Neurotoxicology , vol.15 , pp. 95-107
    • Heidemann, S.R.1    Buxbaum, R.E.2
  • 19
    • 0037122879 scopus 로고    scopus 로고
    • Pathfinding and error correction by retinal axons: The role of astray/robo2
    • Hutson, L.D., and C.-B. Chien. 2002. Pathfinding and error correction by retinal axons: the role of astray/robo2. Neuron. 33:205-217.
    • (2002) Neuron , vol.33 , pp. 205-217
    • Hutson, L.D.1    Chien, C.-B.2
  • 20
    • 0033869644 scopus 로고    scopus 로고
    • The clutch hypothesis revisited: Ascribing the roles of actin-associated proteins in filopodial protrusion in the nerve growth cone
    • Jay, D.G. 2000. The clutch hypothesis revisited: ascribing the roles of actin-associated proteins in filopodial protrusion in the nerve growth cone. J. Neurobiol. 44:114-125.
    • (2000) J. Neurobiol. , vol.44 , pp. 114-125
    • Jay, D.G.1
  • 21
    • 0030809301 scopus 로고    scopus 로고
    • Racl mediates collapsin-l-induced growth cone collapse
    • Jin, Z., and S.M. Strittmatter. 1997. Racl mediates collapsin-l-induced growth cone collapse. J. Neurosci. 17:6256-6263.
    • (1997) J. Neurosci. , vol.17 , pp. 6256-6263
    • Jin, Z.1    Strittmatter, S.M.2
  • 22
    • 0029860810 scopus 로고    scopus 로고
    • Prostaglandin E receptor EP3 subtype induces neurite retraction via small GTPase Rho
    • Katoh, H., M. Negishi, and A. Ichikawa. 1996. Prostaglandin E receptor EP3 subtype induces neurite retraction via small GTPase Rho. J. Biol. Chem. 271:29780-29784.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29780-29784
    • Katoh, H.1    Negishi, M.2    Ichikawa, A.3
  • 23
    • 0032579378 scopus 로고    scopus 로고
    • p160 RhoA-binding kinase ROKalpha induces neurite retraction
    • Katoh, H., J. Aoki, A. Ichikawa, and M. Negishi. 1998. p160 RhoA-binding kinase ROKalpha induces neurite retraction. J. Biol. Chem. 273:2489-2492.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2489-2492
    • Katoh, H.1    Aoki, J.2    Ichikawa, A.3    Negishi, M.4
  • 24
    • 0023664006 scopus 로고
    • The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence
    • Kemp, B.E., R.B. Pearson, V. Guerriero Jr., I.C. Bagchi, and A.R. Means. 1987. The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. J. Biol. Chem. 262:2542-2548.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2542-2548
    • Kemp, B.E.1    Pearson, R.B.2    Guerriero V., Jr.3    Bagchi, I.C.4    Means, A.R.5
  • 25
    • 0023645552 scopus 로고
    • Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain
    • Kennelly, P.J., A.M. Edelman, D.K. Blumenthal, and E.G. Krebs . 1987. Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain. J. Biol. Chem. 262:11958-11963.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11958-11963
    • Kennelly, P.J.1    Edelman, A.M.2    Blumenthal, D.K.3    Krebs, E.G.4
  • 27
    • 0031027205 scopus 로고    scopus 로고
    • Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Racl, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
    • Kozma, R., S. Sarner, S. Ahmed, and L. Lim. 1997. Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Racl, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol. Cell. Biol. 17:1201-1211.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 28
    • 0033018626 scopus 로고    scopus 로고
    • Activation of RhoA by lysophosphatidic acid and Galphal2/13 subunits in neuronal cells: Induction of neurite retraction
    • Kranenburg, O., M. Poland, F.P. van Horck, D. Drechsel, A. Hall, and W.H. Moolenaar. 1999. Activation of RhoA by lysophosphatidic acid and Galphal2/13 subunits in neuronal cells: induction of neurite retraction. Mol. Biol. Cell. 10:1851-1857.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1851-1857
    • Kranenburg, O.1    Poland, M.2    Van Horck, F.P.3    Drechsel, D.4    Hall, A.5    Moolenaar, W.H.6
  • 29
    • 0022106730 scopus 로고
    • Role of myosin light-chain phosphorylation and microtubules in stress fiber morphology in cultured mesangial cells
    • Kreisberg, J.I., M.A. Venkatachalam, R.A. Radnik, and P.Y. Patel. 1985. Role of myosin light-chain phosphorylation and microtubules in stress fiber morphology in cultured mesangial cells. Am. J. Physiol. 249:F227-F235.
    • (1985) Am. J. Physiol. , vol.249
    • Kreisberg, J.I.1    Venkatachalam, M.A.2    Radnik, R.A.3    Patel, P.Y.4
  • 30
    • 0024381605 scopus 로고
    • Direct evidence that growth cones pull
    • Lamoureux, P., R.E. Buxbaum, and S.R. Heidemann. 1989. Direct evidence that growth cones pull. Nature. 340:159-162.
    • (1989) Nature , vol.340 , pp. 159-162
    • Lamoureux, P.1    Buxbaum, R.E.2    Heidemann, S.R.3
  • 31
    • 0033994388 scopus 로고    scopus 로고
    • Regulation of calcineurin by growth cone calcium waves controls neurite extension
    • Lautermilch, N.J., and N.C. Spitzer. 2000. Regulation of calcineurin by growth cone calcium waves controls neurite extension. J. Neurosci. 20:315-325.
    • (2000) J. Neurosci. , vol.20 , pp. 315-325
    • Lautermilch, N.J.1    Spitzer, N.C.2
  • 32
    • 0031914182 scopus 로고    scopus 로고
    • Formation of F-actin aggregates in cells treated with acrin stabilizing drugs
    • Lee, E., E.A. Shelden, and D.A. Knecht. 1998. Formation of F-actin aggregates in cells treated with acrin stabilizing drugs. Cell Motil. Cytoskeleton. 39:122-133.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 122-133
    • Lee, E.1    Shelden, E.A.2    Knecht, D.A.3
  • 33
    • 0019881474 scopus 로고
    • Immunocytochemical evidence for colocalization in neurite growth cones of actin and myosin and their relationship to cell-substratum adhesions
    • Letourneau, P.C. 1981. Immunocytochemical evidence for colocalization in neurite growth cones of actin and myosin and their relationship to cell-substratum adhesions. Dev. Biol. 85:113-122.
    • (1981) Dev. Biol. , vol.85 , pp. 113-122
    • Letourneau, P.C.1
  • 34
    • 0024566580 scopus 로고
    • Distribution and possible interactions of actin-associated proteins and cell adhesion molecules in nerve growth cones
    • Letourneau, P.C., and T.A. Shattuck. 1989. Distribution and possible interactions of actin-associated proteins and cell adhesion molecules in nerve growth cones. Development. 105:505-519.
    • (1989) Development , vol.105 , pp. 505-519
    • Letourneau, P.C.1    Shattuck, T.A.2
  • 35
    • 0023490545 scopus 로고
    • "Pull" and "push" in neurite elongation: Observations on the effects of different concentrations of cytochalasin B and taxol
    • Letourneau, P.C., T.A. Shattuck, and A.H. Ressler. 1989. "Pull" and "push" in neurite elongation: observations on the effects of different concentrations of cytochalasin B and taxol. Cell Motil. Cytoskeleton. 8:193-209.
    • (1989) Cell Motil. Cytoskeleton , vol.8 , pp. 193-209
    • Letourneau, P.C.1    Shattuck, T.A.2    Ressler, A.H.3
  • 36
    • 0029863153 scopus 로고    scopus 로고
    • Myosin drives retrograde F-actin flow in neuronal growth cones
    • Lin, C.H., E.M. Espreafico, M.S. Mooseker, and P. Forscher. 1996. Myosin drives retrograde F-actin flow in neuronal growth cones. Neuron. 16:769-782.
    • (1996) Neuron , vol.16 , pp. 769-782
    • Lin, C.H.1    Espreafico, E.M.2    Mooseker, M.S.3    Forscher, P.4
  • 37
    • 0032825265 scopus 로고    scopus 로고
    • Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
    • Mallavarapu, A., and T. Mitchison. 1999. Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J. Cell Biol. 146:1097-1106.
    • (1999) J. Cell Biol. , vol.146 , pp. 1097-1106
    • Mallavarapu, A.1    Mitchison, T.2
  • 38
    • 0025057070 scopus 로고
    • Turnover of fluorescently labelled tubulin and actin in the axon
    • Okabe, S., and N. Hirokawa. 1990. Turnover of fluorescently labelled tubulin and actin in the axon. Nature. 343:479-482.
    • (1990) Nature , vol.343 , pp. 479-482
    • Okabe, S.1    Hirokawa, N.2
  • 39
    • 0032966750 scopus 로고    scopus 로고
    • Eph receptors and ephrins in neural development
    • O'Leary, D.D., and D.G. Wilkinson. 1999. Eph receptors and ephrins in neural development. Curr. Opin. Neurobiol. 9:65-73.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 65-73
    • O'Leary, D.D.1    Wilkinson, D.G.2
  • 40
    • 0030929986 scopus 로고    scopus 로고
    • The Eph receptor family: Axonal guidance by contact repulsion
    • Orioli, D., and R. Klein. 1997. The Eph receptor family: axonal guidance by contact repulsion. Trends Genet. 13:354-359.
    • (1997) Trends Genet , vol.13 , pp. 354-359
    • Orioli, D.1    Klein, R.2
  • 41
  • 42
    • 0029586312 scopus 로고
    • Localization of myosin II A and B isoforms in cultured neurons
    • Rochlin, M.W., K. Itoh, R.S. Adelstein, and P.C. Bridgman. 1995. Localization of myosin II A and B isoforms in cultured neurons. J. Cell Sci. 108:3661-3670.
    • (1995) J. Cell Sci. , vol.108 , pp. 3661-3670
    • Rochlin, M.W.1    Itoh, K.2    Adelstein, R.S.3    Bridgman, P.C.4
  • 43
    • 0031009586 scopus 로고    scopus 로고
    • Myosin functions in Xenopus retinal ganglion cell growth cone motility in vivo
    • Ruchhoeft, M.L., and W.A. Harris. 1997. Myosin functions in Xenopus retinal ganglion cell growth cone motility in vivo. J. Neurobiol. 32:567-578.
    • (1997) J. Neurobiol. , vol.32 , pp. 567-578
    • Ruchhoeft, M.L.1    Harris, W.A.2
  • 44
    • 0033868010 scopus 로고    scopus 로고
    • Substrate-cytoskeletal coupling as a mechanism for the regulation of growth cone motility and guidance
    • Suter, D.M., and P. Forscher. 2000. Substrate-cytoskeletal coupling as a mechanism for the regulation of growth cone motility and guidance. J. Neurobiol. 44:97-113.
    • (2000) J. Neurobiol. , vol.44 , pp. 97-113
    • Suter, D.M.1    Forscher, P.2
  • 45
    • 0034678363 scopus 로고    scopus 로고
    • Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase
    • Wahl, S., H. Barth, T. Ciossek, K. Aktories, and B.K. Mueller. 2000. Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase. J. Cell Biol. 149:263-270.
    • (2000) J. Cell Biol. , vol.149 , pp. 263-270
    • Wahl, S.1    Barth, H.2    Ciossek, T.3    Aktories, K.4    Mueller, B.K.5
  • 46
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • Watanabe, N., and T.J. Mitchison. 2002. Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science. 295:1083-1086.
    • (2002) Science , vol.295 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 47
    • 0035146457 scopus 로고    scopus 로고
    • Separate but linked functions of conventional myosins modulate adhesion and neurite outgrowth
    • Wylie, S.R., and P.D. Chantler. 2001. Separate but linked functions of conventional myosins modulate adhesion and neurite outgrowth. Nat. Cell Biol. 3:88-92.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 88-92
    • Wylie, S.R.1    Chantler, P.D.2
  • 48
    • 0034810439 scopus 로고    scopus 로고
    • RhoA/rho-associated kinase mediates fibroblast contractile force generation
    • Yee, H.F., Jr., A.C. Melton, and B.N. Tran. 2001. RhoA/rho-associated kinase mediates fibroblast contractile force generation. Biochem. Biophys. Res. Commun. 280:1340-1345.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 1340-1345
    • Yee H.F., Jr.1    Melton, A.C.2    Tran, B.N.3


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