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Volumn 40, Issue 2, 1996, Pages 195-202

Use of a two-hybrid system to investigate molecular interactions of GAP-43

Author keywords

Calmodulin; Development; GAP 43; Growth cone; Phosphoprotein; Protein kinase C; Two hybrid system

Indexed keywords

ASPARTIC ACID; CALMODULIN; NEUROMODULIN; PHOSPHOPROTEIN; PROTEIN KINASE C; SERINE;

EID: 0007465152     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0169-328X(96)00049-6     Document Type: Article
Times cited : (20)

References (57)
  • 1
    • 0028866034 scopus 로고
    • Overexpression of the neural growth-associated protein GAP-43 induces nerve sprouting in the adult nervous system of transgenic mice
    • Aigner L., Arber S., Kapfhammer J.P., Laux T., Schneider C., Botteri F., Brenner H.-R., Caroni P. Overexpression of the neural growth-associated protein GAP-43 induces nerve sprouting in the adult nervous system of transgenic mice. Cell. 83:1995;269-278.
    • (1995) Cell , vol.83 , pp. 269-278
    • Aigner, L.1    Arber, S.2    Kapfhammer, J.P.3    Laux, T.4    Schneider, C.5    Botteri, F.6    Brenner, H.-R.7    Caroni, P.8
  • 2
    • 0027360088 scopus 로고
    • Depletion of 43-kD growth-associated protein in primary sensory neurons leads to diminished formation and spreading of growth cones
    • Aigner L., Caroni P. Depletion of 43-kD growth-associated protein in primary sensory neurons leads to diminished formation and spreading of growth cones. J. Cell Biol. 123:1993;417-429.
    • (1993) J. Cell Biol. , vol.123 , pp. 417-429
    • Aigner, L.1    Caroni, P.2
  • 4
    • 0020827105 scopus 로고
    • Phosphorylaion of B-50 protein by calcium-activated, phospholipid-dependent kinase and B-50 protein kinase
    • Aloyo V.J., Zwiers H., Gispen W.H. Phosphorylaion of B-50 protein by calcium-activated, phospholipid-dependent kinase and B-50 protein kinase. J. Neurochem. 41:1983;649-653.
    • (1983) J. Neurochem , vol.41 , pp. 649-653
    • Aloyo, V.J.1    Zwiers, H.2    Gispen, W.H.3
  • 5
    • 0020618174 scopus 로고
    • Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes
    • Andreasen T.J., Luetje C.W., Heideman W., Storm D.R. Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry. 22:1983;4615-4618.
    • (1983) Biochemistry , vol.22 , pp. 4615-4618
    • Andreasen, T.J.1    Luetje, C.W.2    Heideman, W.3    Storm, D.R.4
  • 6
    • 0025239505 scopus 로고
    • Identification of the protein kinase C phosphorylation site in neuromodulin
    • Apel E.D., Byford M.F., Au D., Walsh K.A., Storm D.R. Identification of the protein kinase C phosphorylation site in neuromodulin. Biochemistry. 29:1990;2330-2335.
    • (1990) Biochemistry , vol.29 , pp. 2330-2335
    • Apel, E.D.1    Byford, M.F.2    Au, D.3    Walsh, K.A.4    Storm, D.R.5
  • 9
    • 0025961398 scopus 로고
    • Purification and characterization of a brain-specific protein kinase C substrate, neurogranin
    • Baudier J., Deloulme J.C., Dorsselaer A.V., Black D.D., Matthes H.W.D. Purification and characterization of a brain-specific protein kinase C substrate, neurogranin. J. Biol. Chem. 266:1991;229-237.
    • (1991) J. Biol. Chem. , vol.266 , pp. 229-237
    • Baudier, J.1    Deloulme, J.C.2    Dorsselaer, A.V.3    Black, D.D.4    Matthes, H.W.D.5
  • 10
    • 0000636606 scopus 로고
    • A membrane phosphoprotein associated with neural development, axonal regeneration, phospholipid metabolism, and synaptic plasticity
    • Benowitz L.I., Routtenberg A. A membrane phosphoprotein associated with neural development, axonal regeneration, phospholipid metabolism, and synaptic plasticity. Trends Neurosci. 10:1987;527-532.
    • (1987) Trends Neurosci , vol.10 , pp. 527-532
    • Benowitz, L.I.1    Routtenberg, A.2
  • 12
    • 0024535737 scopus 로고
    • Bird ED Localization of the growth-associated phosphoprotein GAP-43 in the human cerebral cortex
    • Benowitz L.I., Perrone-Bizzozerro N.I., Finklestein SP Bird ED Localization of the growth-associated phosphoprotein GAP-43 in the human cerebral cortex. J. Neurosci. 9:1989;990-995.
    • (1989) J. Neurosci , vol.9 , pp. 990-995
    • Benowitz, L.I.1    Perrone-Bizzozerro, N.I.2    Finklestein, S.P.3
  • 13
    • 0025365304 scopus 로고
    • The pattern of GAP-43 immunostaining changes in the rat hippocampal formation during reactive synaptogenesis
    • Benowitz L.I., Rodriguez W., Neve R.L. The pattern of GAP-43 immunostaining changes in the rat hippocampal formation during reactive synaptogenesis. Mol. Brain Res. 8:1990;17-23.
    • (1990) Mol. Brain Res. , vol.8 , pp. 17-23
    • Benowitz, L.I.1    Rodriguez, W.2    Neve, R.L.3
  • 14
    • 0022328481 scopus 로고
    • A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressor
    • Brent R., Ptashne M. A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressor. Cell. 43:1985;729-736.
    • (1985) Cell , vol.43 , pp. 729-736
    • Brent, R.1    Ptashne, M.2
  • 15
    • 0026354567 scopus 로고
    • Mutagenesis of the calmodulin binding domain of neuromodulin
    • Chapman E.R., Au D., Nicolson T.A., Storm D.R. Mutagenesis of the calmodulin binding domain of neuromodulin. Prog. Brain Res. 89:1991;37-44.
    • (1991) Prog. Brain Res. , vol.89 , pp. 37-44
    • Chapman, E.R.1    Au, D.2    Nicolson, T.A.3    Storm, D.R.4
  • 17
    • 0026032184 scopus 로고
    • B-50 (GAP-43): Biochemistry and functional neurochemistry of a neuron-specific phosphoprotein
    • Coggins P.J., Zwiers H. B-50 (GAP-43): Biochemistry and functional neurochemistry of a neuron-specific phosphoprotein. J. Neurochem. 56:1991;1095-1106.
    • (1991) J. Neurochem. , vol.56 , pp. 1095-1106
    • Coggins, P.J.1    Zwiers, H.2
  • 18
    • 0027464246 scopus 로고
    • ADP-ribosylation of the neuronal phosphoprotein B-50/GAP-43
    • Coggins P.J., McLean K., Nagy A., Zwiers H. ADP-ribosylation of the neuronal phosphoprotein B-50/GAP-43. J. Neurochem. 60:1993;368-371.
    • (1993) J. Neurochem , vol.60 , pp. 368-371
    • Coggins, P.J.1    McLean, K.2    Nagy, A.3    Zwiers, H.4
  • 19
    • 0026034772 scopus 로고
    • Mapping the development of the rat brain by GAP-43 immunocytochemistry
    • Dani J.W., Armstrong D.M., Benowitz L.I. Mapping the development of the rat brain by GAP-43 immunocytochemistry. Neuroscience. 40:1991;277-288.
    • (1991) Neuroscience , vol.40 , pp. 277-288
    • Dani, J.W.1    Armstrong, D.M.2    Benowitz, L.I.3
  • 20
    • 0025640844 scopus 로고
    • Evidence for the binding of calmodulin to endogenous B-50 (GAP-43) in native synaptosomal plasma membranes
    • DeGraan P.N.E., Oestreicher A.B., DeWit M., Kroef M., Schrama L., Gispen W.H. Evidence for the binding of calmodulin to endogenous B-50 (GAP-43) in native synaptosomal plasma membranes. J. Neurochem. 55:1990;2139-2141.
    • (1990) J. Neurochem. , vol.55 , pp. 2139-2141
    • DeGraan, P.N.E.1    Oestreicher, A.B.2    DeWit, M.3    Kroef, M.4    Schrama, L.5    Gispen, W.H.6
  • 21
    • 0025220414 scopus 로고
    • Depolarization-induced phosphorylation of the protein kinase C substrate B-50 (GAP-43) in rat cortical synaptosomes
    • Dekker L.V., DeGraan P.N.E., DeWit M., Hens J.J.H., Gispen W.H. Depolarization-induced phosphorylation of the protein kinase C substrate B-50 (GAP-43) in rat cortical synaptosomes. J. Neurochem. 54:1989;1645-1652.
    • (1989) J. Neurochem , vol.54 , pp. 1645-1652
    • Dekker, L.V.1    DeGraan, P.N.E.2    DeWit, M.3    Hens, J.J.H.4    Gispen, W.H.5
  • 22
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains
    • Espreafico E.M., Cheney R.E., Matteoli M., Nascimento A.A., De Camilli P.V., Larson R.E., Mooseker M.S. Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J. Cell Biol. 119:1992;1541-1557.
    • (1992) J. Cell Biol. , vol.119 , pp. 1541-1557
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.4    De Camilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 23
    • 85030274957 scopus 로고    scopus 로고
    • Correlation of two hybrid affinity data with in vitro measurements.
    • submitted.
    • Estojak, J., Brent, R. and Golemis, E.A. Correlation of two hybrid affinity data with in vitro measurements. Mol. Cell. Biol. submitted.
    • Mol. Cell. Biol.
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 24
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 340:1989;245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 25
    • 0028568056 scopus 로고
    • Interaction mating reveals binary and ternary connections between drosophila cell cycle regulators
    • Finley R., Brent R. Interaction mating reveals binary and ternary connections between drosophila cell cycle regulators. Proc. Natl. Acad. Sci. USA. 91:1994;12980-12984.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12980-12984
    • Finley, R.1    Brent, R.2
  • 27
    • 0026680723 scopus 로고
    • Fused protein domains inhibit DNA binding by LexA
    • Golemis E.A., Brent R. Fused protein domains inhibit DNA binding by LexA. Mol. Cell Biol. 12:1992;3006-3014.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3006-3014
    • Golemis, E.A.1    Brent, R.2
  • 28
    • 0027437850 scopus 로고
    • Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris J., Golemnis E., Chertkov H., Brent R. Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell. 75:1993;791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemnis, E.2    Chertkov, H.3    Brent, R.4
  • 29
    • 0026633578 scopus 로고
    • Protein phsophatases 1 and 2A dephosphorylate B-50 in presynaptic plasma membranes from rat brain
    • Han Y.F., Wei W., Schlender K.K., Ganjeizadeh M., Dokas L. Protein phsophatases 1 and 2A dephosphorylate B-50 in presynaptic plasma membranes from rat brain. J. Neurochem. 59:1992;364-374.
    • (1992) J. Neurochem , vol.59 , pp. 364-374
    • Han, Y.F.1    Wei, W.2    Schlender, K.K.3    Ganjeizadeh, M.4    Dokas, L.5
  • 30
    • 0027515272 scopus 로고
    • B-50/GAP-43 binds to actin filaments without affecting actin polymerization and filament organization
    • Hens J.J.H., Benfenati F., Nielander H.B., Valotrta F., Gispen W.H., DeGraan P.N.E. B-50/GAP-43 binds to actin filaments without affecting actin polymerization and filament organization. J. Neurochem. 61:1993;1530-1533.
    • (1993) J. Neurochem. , vol.61 , pp. 1530-1533
    • Hens, J.J.H.1    Benfenati, F.2    Nielander, H.B.3    Valotrta, F.4    Gispen, W.H.5    DeGraan, P.N.E.6
  • 31
    • 0022900619 scopus 로고
    • A protein associated with axon growth, GAP-43, is widely distributed and developmentally regulated in rat CNS
    • Jacobson R.D., Virag I., Skene J.H.P. A protein associated with axon growth, GAP-43, is widely distributed and developmentally regulated in rat CNS. J. Neurosci. 6:1986;1843-1855.
    • (1986) J. Neurosci , vol.6 , pp. 1843-1855
    • Jacobson, R.D.1    Virag, I.2    Skene, J.H.P.3
  • 32
    • 0019305702 scopus 로고
    • Modulation of brain polyphosphoinositide metabolism by ACTH-sensitive protein phosphorylation.
    • Jolles J., Zwiers H., van Dongen C.J., Schotman P., Wirtz K.W.A., Gispen W.H. Modulation of brain polyphosphoinositide metabolism by ACTH-sensitive protein phosphorylation. Nature. 286:1980;623-625.
    • (1980) Nature , vol.286 , pp. 623-625
    • Jolles, J.1    Zwiers, H.2    Van Dongen, C.J.3    Schotman, P.4    Wirtz, K.W.A.5    Gispen, W.H.6
  • 34
    • 0024727509 scopus 로고
    • Selective conservation of GAP-43 structure in vertebrate evolution
    • LaBate M.E., Skene J.H.P. Selective conservation of GAP-43 structure in vertebrate evolution. Neuron. 3:1989;299-310.
    • (1989) Neuron , vol.3 , pp. 299-310
    • LaBate, M.E.1    Skene, J.H.P.2
  • 35
    • 0024307526 scopus 로고
    • Dephosphorylation of neuromodulin by calcineurin
    • Liu Y., Storm D.R. Dephosphorylation of neuromodulin by calcineurin. J. Biol. Chem. 264:1989;12800-12804.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12800-12804
    • Liu, Y.1    Storm, D.R.2
  • 36
    • 0022270629 scopus 로고
    • A selective increase in phosphorylation of protein F1, a protein kinase C substrate, directly related to three day growth of long term synaptic enhancement
    • Lovinger D.M., Akers R.F., Nelson R.B., Barnes C.A., McNaughton B.L., Routtenberg A. A selective increase in phosphorylation of protein F1, a protein kinase C substrate, directly related to three day growth of long term synaptic enhancement. Brain Res. 343:1985;137-143.
    • (1985) Brain Res. , vol.343 , pp. 137-143
    • Lovinger, D.M.1    Akers, R.F.2    Nelson, R.B.3    Barnes, C.A.4    McNaughton, B.L.5    Routtenberg, A.6
  • 37
    • 0011060784 scopus 로고
    • Growth-associated protein, GAP-43, a polypeptide that is induced when neurons extend axons, is a component of growth cones and corresponds to pp46, a major polypeptide of a subcellular fraction enriched in growth cones
    • Meiri K.F., Pfenninger K.H., Willard M.B. Growth-associated protein, GAP-43, a polypeptide that is induced when neurons extend axons, is a component of growth cones and corresponds to pp46, a major polypeptide of a subcellular fraction enriched in growth cones. Proc. Natl. Acad. Sci. USA. 83:1986;3537-3541.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3537-3541
    • Meiri, K.F.1    Pfenninger, K.H.2    Willard, M.B.3
  • 38
    • 0025190597 scopus 로고
    • GAP-43 in growth cones is associated with areas of membrane that are tightly bound to substrate and is a component of a membrane skeleton subcellular fraction
    • Meiri K.F., Gordon-Weeks P.R. GAP-43 in growth cones is associated with areas of membrane that are tightly bound to substrate and is a component of a membrane skeleton subcellular fraction. J. Neurosci. 10:1990;156-266.
    • (1990) J. Neurosci , vol.10 , pp. 156-266
    • Meiri, K.F.1    Gordon-Weeks, P.R.2
  • 39
    • 0028141708 scopus 로고
    • Igloo, a GAP-43-related gene expressed in the developing nervous system of drosophila
    • Neel V.A., Young M.W. Igloo, a GAP-43-related gene expressed in the developing nervous system of drosophila. Development. 120:1994;2235-2243.
    • (1994) Development , vol.120 , pp. 2235-2243
    • Neel, V.A.1    Young, M.W.2
  • 40
    • 0023238518 scopus 로고
    • Gradients of protein kinase C substrate phosphorylation in primate visual system peak in visual memory storage areas
    • Nelson R.B., Friedman D.P., O'Neill J.B., Mishkin M., Routtenberg A. Gradients of protein kinase C substrate phosphorylation in primate visual system peak in visual memory storage areas. Brain Res. 416:1987;387-392.
    • (1987) Brain Res , vol.416 , pp. 387-392
    • Nelson, R.B.1    Friedman, D.P.2    O'Neill, J.B.3    Mishkin, M.4    Routtenberg, A.5
  • 43
    • 0027768695 scopus 로고
    • Dependence of calmodulin localization in the retina on the NINAC unconventional myosin
    • Porter J.A., Yu M., Doberstein S.K., Pollard T.D., Montell C. Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science. 262:1993;1038-1042.
    • (1993) Science , vol.262 , pp. 1038-1042
    • Porter, J.A.1    Yu, M.2    Doberstein, S.K.3    Pollard, T.D.4    Montell, C.5
  • 44
    • 0025990516 scopus 로고
    • Phospholipid-mediated delivery of anti-GAP-43 antibodies into neuroblastoma cells prevents neuritogenesis
    • Shea T.B., Perrone-Bizzozerro N.I., Beermann M.L., Benowitz L.I. Phospholipid-mediated delivery of anti-GAP-43 antibodies into neuroblastoma cells prevents neuritogenesis. J. Neurosci. 11:1991;1685-1690.
    • (1991) J. Neurosci , vol.11 , pp. 1685-1690
    • Shea, T.B.1    Perrone-Bizzozerro, N.I.2    Beermann, M.L.3    Benowitz, L.I.4
  • 46
    • 0024508661 scopus 로고
    • Axonal growth-associated proteins
    • Skene J.H.P. Axonal growth-associated proteins. Annu. Rev. Neurosci. 12:1989;127-156.
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 127-156
    • Skene, J.H.P.1
  • 47
    • 0028199935 scopus 로고
    • Neuromodulin (GAP-43) can regulate a calmodulin target in vitro
    • Slemmon J.R., Martzen M.R. Neuromodulin (GAP-43) can regulate a calmodulin target in vitro. Biochemistry. 33:1994;5653-5660.
    • (1994) Biochemistry , vol.33 , pp. 5653-5660
    • Slemmon, J.R.1    Martzen, M.R.2
  • 51
    • 0028021757 scopus 로고
    • A mass spectrometric study on the in vivo posttranslational modification of GAP-43
    • Taniguchi H., Suzuki M., Manenti S., Titani K. A mass spectrometric study on the in vivo posttranslational modification of GAP-43. J. Biol. Chem. 269:1994;22481-22484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22481-22484
    • Taniguchi, H.1    Suzuki, M.2    Manenti, S.3    Titani, K.4
  • 52
    • 0024345452 scopus 로고
    • Muscarinic receptor activation stimulates B-50/GAP-43 phosphorylation in isolated nerve growth cones
    • Van Hooff C.O.M., DeGraan P.N.E., Oestreicher A.B., Gispen W.H. Muscarinic receptor activation stimulates B-50/GAP-43 phosphorylation in isolated nerve growth cones. J. Neurosci. 9:1989;3753-3760.
    • (1989) J. Neurosci. , vol.9 , pp. 3753-3760
    • Van Hooff, C.O.M.1    DeGraan, P.N.E.2    Oestreicher, A.B.3    Gispen, W.H.4
  • 53
    • 0027439584 scopus 로고
    • Phosphorylation-site mutagenesis of the growth-associated protein GAP-43 modulates its effects on cell spreading and morphology
    • Widmer F., Caroni P. Phosphorylation-site mutagenesis of the growth-associated protein GAP-43 modulates its effects on cell spreading and morphology. J. Cell Biol. 120:1993;503-512.
    • (1993) J. Cell Biol. , vol.120 , pp. 503-512
    • Widmer, F.1    Caroni, P.2
  • 54
    • 0028924171 scopus 로고
    • Protein-peptide interactions analyzed with the yeast two-hybrid system
    • Yang M., Wu Z., Fields S. Protein-peptide interactions analyzed with the yeast two-hybrid system. Nucleic Acids Res. 23:1995;1152-1156.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1152-1156
    • Yang, M.1    Wu, Z.2    Fields, S.3
  • 55
    • 0025133998 scopus 로고
    • Transfection of PC12 cells with the human GAP-43 gene: Effects on neurite outgrowth and regeneration
    • Yankner B.A., Benowitz L.I., Villa-Komaroff L., Neve R.L. Transfection of PC12 cells with the human GAP-43 gene: effects on neurite outgrowth and regeneration. Mol. Brain Res. 7:1990;39-44.
    • (1990) Mol. Brain Res. , vol.7 , pp. 39-44
    • Yankner, B.A.1    Benowitz, L.I.2    Villa-Komaroff, L.3    Neve, R.L.4
  • 56
    • 0027511606 scopus 로고
    • MXI1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
    • Zervos A.S., Gyrius J., Brent R. MXI1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell. 72:1993;223-232.
    • (1993) Cell , vol.72 , pp. 223-232
    • Zervos, A.S.1    Gyrius, J.2    Brent, R.3
  • 57
    • 0024390818 scopus 로고
    • The neuronal growth-associated protein GAP-43 induces filopodia in non-neuronal cells
    • Zuber M.X., Goodman D.W., Karns L.R., Fishman M.C. The neuronal growth-associated protein GAP-43 induces filopodia in non-neuronal cells. Science. 244:1989;1193-1195.
    • (1989) Science , vol.244 , pp. 1193-1195
    • Zuber, M.X.1    Goodman, D.W.2    Karns, L.R.3    Fishman, M.C.4


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