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Volumn 139, Issue 4, 1997, Pages 951-961

Neurabin: A novel neural tissue-specific actin filament-binding protein involved in neurite formation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; F ACTIN;

EID: 0030682482     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.4.951     Document Type: Article
Times cited : (168)

References (58)
  • 1
    • 0028097090 scopus 로고
    • Hippocampal synaptogenesis in cell culture: Developmental time course of synapse formation, calcium influx, and synaptic protein distribution
    • Basarsky, T.A., V. Parpura, and P.G. Haydon. 1994. Hippocampal synaptogenesis in cell culture: developmental time course of synapse formation, calcium influx, and synaptic protein distribution. J. Neurosci. 14:6402-6411.
    • (1994) J. Neurosci. , vol.14 , pp. 6402-6411
    • Basarsky, T.A.1    Parpura, V.2    Haydon, P.G.3
  • 3
    • 0023027034 scopus 로고
    • Disoriented pathfinding by pioneer neurone growth cones deprived of filopodia by cytochalasin treatment
    • Bentley, D., and A. Toroian-Raymond. 1986. Disoriented pathfinding by pioneer neurone growth cones deprived of filopodia by cytochalasin treatment. Nature. 323:712-715.
    • (1986) Nature , vol.323 , pp. 712-715
    • Bentley, D.1    Toroian-Raymond, A.2
  • 4
    • 0028126032 scopus 로고
    • Cytoskeletal events in growth cone steering
    • Bentley, D., and T.P. O'Connor. 1994. Cytoskeletal events in growth cone steering. Curr. Opin. Neurobiol. 4:43-48.
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 43-48
    • Bentley, D.1    O'Connor, T.P.2
  • 5
    • 0028914466 scopus 로고
    • The role of agrin in synapse formation
    • Bowe, M.A., and J.R. Fallon. 1995. The role of agrin in synapse formation. Annu. Rev. Neurosci. 18:443-462.
    • (1995) Annu. Rev. Neurosci. , vol.18 , pp. 443-462
    • Bowe, M.A.1    Fallon, J.R.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0028810956 scopus 로고
    • Synaptic structure and function: Dynamic organization yields architectural precision
    • Burns, M.E., and G.J. Augustine. 1995. Synaptic structure and function: dynamic organization yields architectural precision. Cell. 83:187-194.
    • (1995) Cell , vol.83 , pp. 187-194
    • Burns, M.E.1    Augustine, G.J.2
  • 8
    • 0026026620 scopus 로고
    • Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein
    • Chia, C.P., A.L. Hitt, and E.J. Luna. 1991. Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein. Cell Motil. Cytoskeleton. 18:164-179.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 164-179
    • Chia, C.P.1    Hitt, A.L.2    Luna, E.J.3
  • 9
    • 0030589638 scopus 로고    scopus 로고
    • Neuronal pathfinding and recognition: Roles of cell adhesion molecules
    • Chiba, A., and H. Keshishian. 1996. Neuronal pathfinding and recognition: roles of cell adhesion molecules. Dev. Biol. 180:424-432.
    • (1996) Dev. Biol. , vol.180 , pp. 424-432
    • Chiba, A.1    Keshishian, H.2
  • 10
    • 0027327185 scopus 로고
    • Navigational errors made by growth cones without filopodia in the embryonic Xenopus brain
    • Chien, C.-B., D.E. Rosenthal, W.A. Harris, and C.E. Holt. 1993. Navigational errors made by growth cones without filopodia in the embryonic Xenopus brain. Neuron. 11:237-251.
    • (1993) Neuron. , vol.11 , pp. 237-251
    • Chien, C.-B.1    Rosenthal, D.E.2    Harris, W.A.3    Holt, C.E.4
  • 11
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila disc-large tumor suppressor protein
    • Cho, K.-O., C.A. Hunt, and M.B. Kennedy. 1992. The rat brain postsynaptic density fraction contains a homolog of the Drosophila disc-large tumor suppressor protein. Neuron. 9:929-942.
    • (1992) Neuron. , vol.9 , pp. 929-942
    • Cho, K.-O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 12
    • 0029971793 scopus 로고    scopus 로고
    • Functions of netrins and semaphorins in axon guidance
    • Culotti, J.G., and A.L. Kolodkin. 1996. Functions of netrins and semaphorins in axon guidance. Curr. Opin. Neurobiol. 6:81-88.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 81-88
    • Culotti, J.G.1    Kolodkin, A.L.2
  • 13
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti, C.G., C.A. Sullivan, and G.A. Banker. 1988. The establishment of polarity by hippocampal neurons in culture. J. Neurosci. 8:1454-1468.
    • (1988) J. Neurosci. , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 14
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., A. Lee, J. Lewis, E. Kim, M. Sheng, and R. MacKinnon. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 15
    • 0020285619 scopus 로고
    • Molecular properties and functions in vitro of chicken smooth-muscle alpha-actinin in comparison with those of striated-muscle alpha-actinins
    • Endo, T., and T. Masaki. 1982. Molecular properties and functions in vitro of chicken smooth-muscle alpha-actinin in comparison with those of striated-muscle alpha-actinins. J. Biochem. (Tokyo). 92:1457-1468.
    • (1982) J. Biochem. (Tokyo) , vol.92 , pp. 1457-1468
    • Endo, T.1    Masaki, T.2
  • 16
    • 0030296833 scopus 로고    scopus 로고
    • Neural cell adhesion molecules in activity-dependent development and synaptic plasticity
    • Fields, R.D., and K. Itoh. 1996. Neural cell adhesion molecules in activity-dependent development and synaptic plasticity. Trends Neurosci. 19:473-480.
    • (1996) Trends Neurosci. , vol.19 , pp. 473-480
    • Fields, R.D.1    Itoh, K.2
  • 17
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organization of actin filaments and microtubles in a neuronal growth cone
    • Forscher, P., and S.J. Smith. 1988. Actions of cytochalasins on the organization of actin filaments and microtubles in a neuronal growth cone. J. Cell Biol. 107:1505-1516.
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 18
    • 0016823377 scopus 로고
    • The interaction of heavy meromyosin and subfragment 1 with actin. Physical measurements in the presence and absence of adenosine triphosphate
    • Fraser, A.B., E. Eisenberg, W.W. Kielley, and F.D. Carlson. 1975. The interaction of heavy meromyosin and subfragment 1 with actin. Physical measurements in the presence and absence of adenosine triphosphate. Biochemistry. 14:2207-2214.
    • (1975) Biochemistry , vol.14 , pp. 2207-2214
    • Fraser, A.B.1    Eisenberg, E.2    Kielley, W.W.3    Carlson, F.D.4
  • 19
    • 0029943807 scopus 로고    scopus 로고
    • Eph receptor tyrosine kinases and their ligands in neural development
    • Friedman, G.C., and D.D.M. O'Leary. 1996. Eph receptor tyrosine kinases and their ligands in neural development. Curr. Opin. Neurobiol. 6:127-133.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 127-133
    • Friedman, G.C.1    O'Leary, D.D.M.2
  • 20
    • 0030296378 scopus 로고    scopus 로고
    • Synaptic proteins and the assembly of synaptic junctions
    • Garner, C.C., and S. Kindler. 1996. Synaptic proteins and the assembly of synaptic junctions. Trends Cell Biol. 6:429-433.
    • (1996) Trends Cell Biol. , vol.6 , pp. 429-433
    • Garner, C.C.1    Kindler, S.2
  • 21
    • 0028810955 scopus 로고
    • Neuronal target recognition
    • Garrity, P.A., and S.L. Zipursky. 1995. Neuronal target recognition. Cell. 83: 177-185.
    • (1995) Cell , vol.83 , pp. 177-185
    • Garrity, P.A.1    Zipursky, S.L.2
  • 22
    • 0024422958 scopus 로고
    • The role of cytoskeleton in organizing growth cones: A microfilament-associated growth cone component depends upon microtubules for its localization
    • Goslin, K., E. Birgbauer, G. Banker, and F. Solomon. 1989. The role of cytoskeleton in organizing growth cones: a microfilament-associated growth cone component depends upon microtubules for its localization. J. Cell Biol. 109: 1621-1631.
    • (1989) J. Cell Biol. , vol.109 , pp. 1621-1631
    • Goslin, K.1    Birgbauer, E.2    Banker, G.3    Solomon, F.4
  • 23
    • 0002329664 scopus 로고
    • Rat hippocampal neurons in low-density culture
    • G. Banker, and K. Goslin, editors. MIT Press, Cambridge, MA
    • Goslin, K., and G. Banker. 1991. Rat hippocampal neurons in low-density culture. In Culturing nerve cells. G. Banker, and K. Goslin, editors. MIT Press, Cambridge, MA. 251-281.
    • (1991) Culturing Nerve Cells , pp. 251-281
    • Goslin, K.1    Banker, G.2
  • 24
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K.L., and J.E. Dixon. 1991. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 26
    • 0028998826 scopus 로고
    • A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic
    • Hata, Y., and T.C. Südhof. 1995. A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic. J. Biol. Chem. 270: 13022-13028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13022-13028
    • Hata, Y.1    Südhof, T.C.2
  • 27
    • 0024595352 scopus 로고
    • The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1
    • Hirokawa, N., K. Sobue, K. Kanda, A. Harada, and H. Yorifuji. 1989. The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1. J. Cell Biol. 108:111-126.
    • (1989) J. Cell Biol. , vol.108 , pp. 111-126
    • Hirokawa, N.1    Sobue, K.2    Kanda, K.3    Harada, A.4    Yorifuji, H.5
  • 28
    • 0028670842 scopus 로고
    • Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells
    • Imazumi, K., T. Sasaki, K. Takahashi, and Y. Takai. 1994. Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells. Biochem. Biophys. Res. Commun. 205:1409-1416.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1409-1416
    • Imazumi, K.1    Sasaki, T.2    Takahashi, K.3    Takai, Y.4
  • 30
    • 0028884221 scopus 로고
    • Axon guidance molecules
    • Keynes, R., and G.M.W. Cook. 1995. Axon guidance molecules. Cell. 83:161-169.
    • (1995) Cell , vol.83 , pp. 161-169
    • Keynes, R.1    Cook, G.M.W.2
  • 33
    • 0024566580 scopus 로고
    • Distribution and possible interactions of actin-associated proteins and cell adhesion molecules of nerve growth cones
    • Letourneau, P.C., and T.A. Shattuck. 1989. Distribution and possible interactions of actin-associated proteins and cell adhesion molecules of nerve growth cones. Development (Camb.). 105:505-519.
    • (1989) Development (Camb.) , vol.105 , pp. 505-519
    • Letourneau, P.C.1    Shattuck, T.A.2
  • 34
    • 0028104673 scopus 로고
    • Cytoskeletal reorganization underlying growth cone motility
    • Lin, C.-H., C.A. Thompson, and P. Forscher. 1994. Cytoskeletal reorganization underlying growth cone motility. Curr. Opin. Neurobiol. 4:640-647.
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 640-647
    • Lin, C.-H.1    Thompson, C.A.2    Forscher, P.3
  • 35
    • 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
  • 36
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science. 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 37
    • 0028829750 scopus 로고
    • The Rho's progress: A potential role during neuritogenesis for the Rho family of GTPases
    • Mackay, D.J.G, C.D. Nobes, and A. Hall. 1995. The Rho's progress: a potential role during neuritogenesis for the Rho family of GTPases. Trends Neurosci. 18:496-501.
    • (1995) Trends Neurosci. , vol.18 , pp. 496-501
    • Mackay, D.J.G.1    Nobes, C.D.2    Hall, A.3
  • 39
    • 0021680448 scopus 로고
    • Growth of neuntes without filopodial or lamellipodial activity in the presence of cytochalasin B
    • Marsh, L., and P.C. Letourneau. 1984. Growth of neuntes without filopodial or lamellipodial activity in the presence of cytochalasin B.J. Cell Biol. 99:2041-2047.
    • (1984) J. Cell Biol. , vol.99 , pp. 2041-2047
    • Marsh, L.1    Letourneau, P.C.2
  • 40
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira, P. 1991. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16:87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 41
    • 0019851385 scopus 로고
    • Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue
    • Matthew, W.D., L. Tsavaler, and L.F. Reichardt. 1981. Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue. J. Cell Biol. 91:257-269.
    • (1981) J. Cell Biol. , vol.91 , pp. 257-269
    • Matthew, W.D.1    Tsavaler, L.2    Reichardt, L.F.3
  • 42
    • 0024109183 scopus 로고
    • Cytoskeletal dynamics and nerve growth
    • Mitchison, T., and M. Kirschner. 1988. Cytoskeletal dynamics and nerve growth. Neuron. 1:761-772.
    • (1988) Neuron. , vol.1 , pp. 761-772
    • Mitchison, T.1    Kirschner, M.2
  • 43
    • 0025334258 scopus 로고
    • Localization and subcellular distribution of smg p25A, a ras p21-like GTP-binding protein, in rat brain
    • Mizoguchi, A., S. Kim, T. Ueda, A. Kikuchi, H. Yorifuji, N. Hirokawa, and Y. Takai. 1990. Localization and subcellular distribution of smg p25A, a ras p21-like GTP-binding protein, in rat brain. J. Biol. Chem. 265:11872-11879.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11872-11879
    • Mizoguchi, A.1    Kim, S.2    Ueda, T.3    Kikuchi, A.4    Yorifuji, H.5    Hirokawa, N.6    Takai, Y.7
  • 44
    • 0023032310 scopus 로고
    • Protein p38: An integral membrane protein specific for small vesicles of neurons and neuroendocrine cells
    • Navone, F., R. Jahn, G. Di Gioia, H. Stukenbrok, P. Greengard, and P. De Camilli. 1986. Protein p38: An integral membrane protein specific for small vesicles of neurons and neuroendocrine cells. J. Cell Biol. 103:2511-2527.
    • (1986) J. Cell Biol. , vol.103 , pp. 2511-2527
    • Navone, F.1    Jahn, R.2    Di Gioia, G.3    Stukenbrok, H.4    Greengard, P.5    De Camilli, P.6
  • 45
  • 47
    • 0020012723 scopus 로고
    • Methods to characterize actin filament networks
    • Pollard, T.D., and J.A. Cooper. 1982. Methods to characterize actin filament networks. Methods Enzymol. 85:211-233.
    • (1982) Methods Enzymol. , vol.85 , pp. 211-233
    • Pollard, T.D.1    Cooper, J.A.2
  • 50
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras, J., and C.-H. Heldin. 1996. PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem. Sci. 21:455-458.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.-H.2
  • 52
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases
    • Siegel, L.M., and K.J. Monty. 1966. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim. Biophys. Acta. 112:346-362.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 53
    • 0023781654 scopus 로고
    • Neuronal cytomechanics: The actin-based motility of growth cones
    • Smith, S.J. 1988. Neuronal cytomechanics: the actin-based motility of growth cones. Science. 242:708-715.
    • (1988) Science , vol.242 , pp. 708-715
    • Smith, S.J.1
  • 55
    • 0030957966 scopus 로고    scopus 로고
    • SAPAPs: A family of PSD-95/SAP90-associated proteins localized at postsynaptic density
    • Takeuchi, M., Y. Hata, K. Hirao, A. Toyoda, M. Irie, and Y. Takai. 1997. SAPAPs: a family of PSD-95/SAP90-associated proteins localized at postsynaptic density. J. Biol. Chem. 272:11943-11951.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11943-11951
    • Takeuchi, M.1    Hata, Y.2    Hirao, K.3    Toyoda, A.4    Irie, M.5    Takai, Y.6
  • 56
    • 0028863477 scopus 로고
    • Making the connection: Cytoskeletal rearrangements during growth cone guidance
    • Tanaka, E., and J. Sabry. 1995. Making the connection: Cytoskeletal rearrangements during growth cone guidance. Cell. 83:171-176.
    • (1995) Cell , vol.83 , pp. 171-176
    • Tanaka, E.1    Sabry, J.2
  • 57
    • 0029959555 scopus 로고    scopus 로고
    • The molecular biology of axon guidance
    • Tessier-Lavigne, M., and C.S. Goodman. 1996. The molecular biology of axon guidance. Science. 274:1123-1133.
    • (1996) Science , vol.274 , pp. 1123-1133
    • Tessier-Lavigne, M.1    Goodman, C.S.2
  • 58
    • 0028670775 scopus 로고
    • Dynamin 1 antisense oligonucleotide treatment prevents neurite formation in cultured hippocampal neurons
    • Torre, E., M.A. Mcniven, and R. Urrutia. 1994. Dynamin 1 antisense oligonucleotide treatment prevents neurite formation in cultured hippocampal neurons. J. Biol. Chem. 269:32411-32417.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32411-32417
    • Torre, E.1    Mcniven, M.A.2    Urrutia, R.3


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