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Volumn 18, Issue 8, 2007, Pages 3131-3143

Fast turnover of L1 adhesions in neuronal growth cones involving both surface diffusion and exo/endocytosis of L1 molecules

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL ADHESION MOLECULE; CLATHRIN; GREEN FLUORESCENT PROTEIN; MICROSPHERE; NERVE CELL ADHESION MOLECULE; PROTEIN L1; QUANTUM DOT; THROMBIN; UNCLASSIFIED DRUG;

EID: 34547731318     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-12-1101     Document Type: Article
Times cited : (41)

References (53)
  • 1
    • 10744223512 scopus 로고    scopus 로고
    • Cross talk between tetanus neurotoxin-insensitive vesicle-associated membrane protein-mediated transport and L1-mediated adhesion
    • Alberts, P. et al. (2003). Cross talk between tetanus neurotoxin-insensitive vesicle-associated membrane protein-mediated transport and L1-mediated adhesion. Mol. Biol. Cell 14, 4207-4220.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4207-4220
    • Alberts, P.1
  • 2
    • 33644852316 scopus 로고    scopus 로고
    • Cdc42 and actin control polarized expression of TI-VAMP vesicles to neuronal growth cones and their fusion with the plasma membrane
    • Alberts, P., Rudge, R., Irinopoulou, T., Danglot, L., Gauthier-Rouviere, C., and Galli, T. (2006). Cdc42 and actin control polarized expression of TI-VAMP vesicles to neuronal growth cones and their fusion with the plasma membrane. Mol. Biol. Cell 17, 1194-1203.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1194-1203
    • Alberts, P.1    Rudge, R.2    Irinopoulou, T.3    Danglot, L.4    Gauthier-Rouviere, C.5    Galli, T.6
  • 3
    • 33846441246 scopus 로고    scopus 로고
    • Ankyrin-dependent and -independent mechanisms orchestrate axonal compartmentalization of L1 family members neurofascin and L1/neuron-glia cell adhesion molecule
    • Boiko, T., Vakulenko, M., Ewers, H., Yap, C. C., Norden, C., and Winckler, B. (2007). Ankyrin-dependent and -independent mechanisms orchestrate axonal compartmentalization of L1 family members neurofascin and L1/neuron-glia cell adhesion molecule. J. Neurosci. 27, 590-603.
    • (2007) J. Neurosci , vol.27 , pp. 590-603
    • Boiko, T.1    Vakulenko, M.2    Ewers, H.3    Yap, C.C.4    Norden, C.5    Winckler, B.6
  • 4
    • 0029938079 scopus 로고    scopus 로고
    • Thrombin causes cell spreading and redistribution of beta-amyloid immunoreactivity in cultured hippocampal neurons
    • Brewer, G. J. (1996). Thrombin causes cell spreading and redistribution of beta-amyloid immunoreactivity in cultured hippocampal neurons. J. Neurochem. 67, 119-130.
    • (1996) J. Neurochem , vol.67 , pp. 119-130
    • Brewer, G.J.1
  • 5
    • 0035479922 scopus 로고    scopus 로고
    • Immunoglobulin superfamily receptors: Cis-interactions, intracellular adapters and alternative splicing regulate adhesion
    • Brummendorf, T., and Lemmon, V. (2001). Immunoglobulin superfamily receptors: cis-interactions, intracellular adapters and alternative splicing regulate adhesion. Curr. Opin. Cell Biol. 13, 611-618.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 611-618
    • Brummendorf, T.1    Lemmon, V.2
  • 6
    • 12144267589 scopus 로고    scopus 로고
    • L1-mediated branching is regulated by two ezrin-radixin-moesin (ERM)-binding sites, the RSLE region and a novel juxtamembrane ERM-binding region
    • Cheng, L., Itoh, K., and Lemmon, V. (2005). L1-mediated branching is regulated by two ezrin-radixin-moesin (ERM)-binding sites, the RSLE region and a novel juxtamembrane ERM-binding region. J. Neurosci. 25, 395-403.
    • (2005) J. Neurosci , vol.25 , pp. 395-403
    • Cheng, L.1    Itoh, K.2    Lemmon, V.3
  • 7
    • 0037096170 scopus 로고    scopus 로고
    • Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation
    • Coussen, F., Choquet, D., Sheetz, M. P., and Erickson, H. P. (2002). Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation. J. Cell Sci. 115, 2581-2590.
    • (2002) J. Cell Sci , vol.115 , pp. 2581-2590
    • Coussen, F.1    Choquet, D.2    Sheetz, M.P.3    Erickson, H.P.4
  • 8
    • 24144497748 scopus 로고    scopus 로고
    • Synapse associated protein 102 is a novel binding partner to the cytoplasmic terminus of neurone-glial related cell adhesion molecule
    • Davey, F., Hill, M., Falk, J., Sans, N., and Gunn-Moore, F. J. (2005). Synapse associated protein 102 is a novel binding partner to the cytoplasmic terminus of neurone-glial related cell adhesion molecule. J. Neurochem. 94, 1243-1253.
    • (2005) J. Neurochem , vol.94 , pp. 1243-1253
    • Davey, F.1    Hill, M.2    Falk, J.3    Sans, N.4    Gunn-Moore, F.J.5
  • 9
    • 0033200228 scopus 로고    scopus 로고
    • Pathological missense mutations of neural cell adhesion molecule L1 affect homophilic and heterophilic binding activities
    • De Angelis, E., MacFarlane, J., Du, J. S., Yeo, G., Hicks, R., Rathjen, F. G., Kenwrick, S., and Brummendorf, T. (1999). Pathological missense mutations of neural cell adhesion molecule L1 affect homophilic and heterophilic binding activities. EMBO J 18, 4744-4753.
    • (1999) EMBO J , vol.18 , pp. 4744-4753
    • De Angelis, E.1    MacFarlane, J.2    Du, J.S.3    Yeo, G.4    Hicks, R.5    Rathjen, F.G.6    Kenwrick, S.7    Brummendorf, T.8
  • 10
    • 0036154050 scopus 로고    scopus 로고
    • Disease-associated mutations in L1 CAM interfere with ligand interactions and cell-surface expression
    • De Angelis, E., Watkins, A., Schafer, M., Brummendorf, T., and Kenwrick, S. (2002). Disease-associated mutations in L1 CAM interfere with ligand interactions and cell-surface expression. Hum. Mol. Genet. 11, 1-12.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1-12
    • De Angelis, E.1    Watkins, A.2    Schafer, M.3    Brummendorf, T.4    Kenwrick, S.5
  • 11
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and axon guidance
    • Dent, E. W., and Gertler, F. B. (2003). Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40, 209-227.
    • (2003) Neuron , vol.40 , pp. 209-227
    • Dent, E.W.1    Gertler, F.B.2
  • 12
    • 0037166931 scopus 로고    scopus 로고
    • Functional binding interaction identified between the axonal CAM L1 and members of the ERM family
    • Dickson, T. C., Mintz, C. D., Benson, D. L., and Salton, S. R. (2002). Functional binding interaction identified between the axonal CAM L1 and members of the ERM family. J. Cell Biol. 157, 1105-1112.
    • (2002) J. Cell Biol , vol.157 , pp. 1105-1112
    • Dickson, T.C.1    Mintz, C.D.2    Benson, D.L.3    Salton, S.R.4
  • 13
    • 0037144811 scopus 로고    scopus 로고
    • Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone
    • Diefenbach, T. J., Latham, V. M., Yimlamai, D., Liu, C. A., Herman, I. M., and Jay, D. G. (2002). Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone. J. Cell Biol. 158, 1207-1217.
    • (2002) J. Cell Biol , vol.158 , pp. 1207-1217
    • Diefenbach, T.J.1    Latham, V.M.2    Yimlamai, D.3    Liu, C.A.4    Herman, I.M.5    Jay, D.G.6
  • 14
    • 16944366731 scopus 로고    scopus 로고
    • Thrombin induces apoptosis in cultured neurons and astrocytes via a pathway requiring tyrosine kinase and RhoA activities
    • Donovan, F. M., Pike, C. J., Cotman, C. W., and Cunningham, D. D. (1997). Thrombin induces apoptosis in cultured neurons and astrocytes via a pathway requiring tyrosine kinase and RhoA activities. J. Neurosci. 17, 5316-5326.
    • (1997) J. Neurosci , vol.17 , pp. 5316-5326
    • Donovan, F.M.1    Pike, C.J.2    Cotman, C.W.3    Cunningham, D.D.4
  • 15
    • 4644258075 scopus 로고    scopus 로고
    • NrCAM coupling to the cytoskeleton depends on multiple protein domains and partitioning into lipid rafts
    • Falk, J., Thoumine, O., Dequidt, C., Choquet, D., and Faivre-Sarrailh, C. (2004). NrCAM coupling to the cytoskeleton depends on multiple protein domains and partitioning into lipid rafts. Mol. Biol. Cell 15, 4695-4709.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4695-4709
    • Falk, J.1    Thoumine, O.2    Dequidt, C.3    Choquet, D.4    Faivre-Sarrailh, C.5
  • 16
    • 0031006110 scopus 로고    scopus 로고
    • Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin
    • Garver, T. D., Ren, Q., Tuvia, S., and Bennett, V. (1997). Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin. J. Cell Biol. 137, 703-714.
    • (1997) J. Cell Biol , vol.137 , pp. 703-714
    • Garver, T.D.1    Ren, Q.2    Tuvia, S.3    Bennett, V.4
  • 17
    • 0042477621 scopus 로고    scopus 로고
    • Ankyrin binding mediates L1CAM interactions with static components of the cytoskeleton and inhibits retrograde movement of L1CAM on the cell surface
    • Gil, O. D., Sakurai, T., Bradley, A. E., Fink, M. Y., Cassella, M. R., Kuo, J. A., and Felsenfeld, D. P. (2003). Ankyrin binding mediates L1CAM interactions with static components of the cytoskeleton and inhibits retrograde movement of L1CAM on the cell surface. J. Cell Biol. 162, 719-730.
    • (2003) J. Cell Biol , vol.162 , pp. 719-730
    • Gil, O.D.1    Sakurai, T.2    Bradley, A.E.3    Fink, M.Y.4    Cassella, M.R.5    Kuo, J.A.6    Felsenfeld, D.P.7
  • 18
    • 0002329664 scopus 로고
    • Rat hippocampal neurons in low-density culture
    • ed. G. Banker and K. Goslin, Cambridge, MA: The MIT Press
    • Goslin, K., Asmussen, H., and Banker, G. (1991). Rat hippocampal neurons in low-density culture. In: Culturing Nerve Cells, ed. G. Banker and K. Goslin, Cambridge, MA: The MIT Press, 339-370.
    • (1991) Culturing Nerve Cells , pp. 339-370
    • Goslin, K.1    Asmussen, H.2    Banker, G.3
  • 19
    • 0034097989 scopus 로고    scopus 로고
    • Trimerization of cell adhesion molecule L1 mimics clustered L1 expression on the cell surface: Influence on L1-ligand interactions and on promotion of neurite outgrowth
    • Hall, H., Bozic, D., Fauser, C., and Engel, J. (2000). Trimerization of cell adhesion molecule L1 mimics clustered L1 expression on the cell surface: influence on L1-ligand interactions and on promotion of neurite outgrowth. J. Neurochem. 75, 336-346.
    • (2000) J. Neurochem , vol.75 , pp. 336-346
    • Hall, H.1    Bozic, D.2    Fauser, C.3    Engel, J.4
  • 20
    • 12844282154 scopus 로고    scopus 로고
    • Distribution of L1cam mRNA in the adult mouse brain: In situ hybridization and Northern blot analyses
    • Horinouchi, K., Nakamura, Y., Yamanaka, H., Watabe, T., and Shiosaka, S. (2005). Distribution of L1cam mRNA in the adult mouse brain: in situ hybridization and Northern blot analyses. J. Comp. Neurol. 482, 386-404.
    • (2005) J. Comp. Neurol , vol.482 , pp. 386-404
    • Horinouchi, K.1    Nakamura, Y.2    Yamanaka, H.3    Watabe, T.4    Shiosaka, S.5
  • 22
    • 19444383222 scopus 로고    scopus 로고
    • Dephosphorylation and internalization of cell adhesion molecule L1 induced by theta burst stimulation in rat hippocampus
    • Itoh, K., Shimono, K., and Lemmon, V. (2005). Dephosphorylation and internalization of cell adhesion molecule L1 induced by theta burst stimulation in rat hippocampus. Mol. Cell Neurosci. 29, 245-249.
    • (2005) Mol. Cell Neurosci , vol.29 , pp. 245-249
    • Itoh, K.1    Shimono, K.2    Lemmon, V.3
  • 23
    • 0031726520 scopus 로고    scopus 로고
    • Role of L1 in neural development: What the knockouts tell us
    • Kamiguchi, H., Hlavin, M. L., and Lemmon, V. (1998a). Role of L1 in neural development: what the knockouts tell us. Mol. Cell Neurosci. 12, 48-55.
    • (1998) Mol. Cell Neurosci , vol.12 , pp. 48-55
    • Kamiguchi, H.1    Hlavin, M.L.2    Lemmon, V.3
  • 24
    • 0034658292 scopus 로고    scopus 로고
    • Recycling of the cell adhesion molecule L1 in axonal growth cones
    • Kamiguchi, H., and Lemmon, V. (2000). Recycling of the cell adhesion molecule L1 in axonal growth cones. J. Neurosci. 20, 3676-3686.
    • (2000) J. Neurosci , vol.20 , pp. 3676-3686
    • Kamiguchi, H.1    Lemmon, V.2
  • 25
    • 0032527593 scopus 로고    scopus 로고
    • The neural cell adhesion molecule L1 interacts with the AP-2 adaptor and is endocytosed via the clathrin-mediated pathway
    • Kamiguchi, H., Long, K. E., Pendergast, M., Schaefer, A. W., Rapoport, I., Kirchhausen, T., and Lemmon, V. (1998b). The neural cell adhesion molecule L1 interacts with the AP-2 adaptor and is endocytosed via the clathrin-mediated pathway. J. Neurosci. 18, 5311-5321.
    • (1998) J. Neurosci , vol.18 , pp. 5311-5321
    • Kamiguchi, H.1    Long, K.E.2    Pendergast, M.3    Schaefer, A.W.4    Rapoport, I.5    Kirchhausen, T.6    Lemmon, V.7
  • 26
    • 0035576278 scopus 로고    scopus 로고
    • The role of endocytic l1 trafficking in polarized adhesion and migration of nerve growth cones
    • Kamiguchi, H., and Yoshihara, F. (2001). The role of endocytic l1 trafficking in polarized adhesion and migration of nerve growth cones. J. Neurosci. 21, 9194-9203.
    • (2001) J. Neurosci , vol.21 , pp. 9194-9203
    • Kamiguchi, H.1    Yoshihara, F.2
  • 27
    • 0035815656 scopus 로고    scopus 로고
    • The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity
    • Koroll, M., Rathjen, F. G., and Volkmer, H. (2001). The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity. J. Biol. Chem. 276, 10646-10654.
    • (2001) J. Biol. Chem , vol.276 , pp. 10646-10654
    • Koroll, M.1    Rathjen, F.G.2    Volkmer, H.3
  • 28
    • 0035846950 scopus 로고    scopus 로고
    • The role of endocytosis in regulating L1-mediated adhesion
    • Long, K. E., Asou, H., Snider, M. D., and Lemmon, V. (2001). The role of endocytosis in regulating L1-mediated adhesion. J. Biol. Chem. 276, 1285-1290.
    • (2001) J. Biol. Chem , vol.276 , pp. 1285-1290
    • Long, K.E.1    Asou, H.2    Snider, M.D.3    Lemmon, V.4
  • 29
    • 33845882730 scopus 로고    scopus 로고
    • Neural recognition molecules of the immunoglobulin superfamily: Signaling transducers of axon guidance and neuronal migration
    • Maness, P. F., and Schachner, M. (2007). Neural recognition molecules of the immunoglobulin superfamily: signaling transducers of axon guidance and neuronal migration. Nat. Neurosci. 10, 19-26.
    • (2007) Nat. Neurosci , vol.10 , pp. 19-26
    • Maness, P.F.1    Schachner, M.2
  • 30
    • 0027533287 scopus 로고
    • Regional distribution of neural cell adhesion molecule (N-CAM) and L1 in human and rodent hippocampus
    • Miller, P. D., Chung, W. W., Lagenaur, C. F., and DeKosky, S. T. (1993). Regional distribution of neural cell adhesion molecule (N-CAM) and L1 in human and rodent hippocampus. J. Comp. Neurol. 327, 341-349.
    • (1993) J. Comp. Neurol , vol.327 , pp. 341-349
    • Miller, P.D.1    Chung, W.W.2    Lagenaur, C.F.3    DeKosky, S.T.4
  • 31
    • 2642543393 scopus 로고    scopus 로고
    • Distribution and densitometry mapping of L1-CAM immunoreactivity in the adult mouse brain-light microscopic observation
    • Munakata, H., Nakamura, Y., Matsumoto-Miyai, K., Itoh, K., Yamasaki, H., and Shiosaka, S. (2003). Distribution and densitometry mapping of L1-CAM immunoreactivity in the adult mouse brain-light microscopic observation. BMC Neurosci. 4, 7.
    • (2003) BMC Neurosci , vol.4 , pp. 7
    • Munakata, H.1    Nakamura, Y.2    Matsumoto-Miyai, K.3    Itoh, K.4    Yamasaki, H.5    Shiosaka, S.6
  • 32
    • 0035283308 scopus 로고    scopus 로고
    • Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions
    • Needham, L. K., Thelen, K., and Maness, P. F. (2001). Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions. J. Neurosci. 21, 1490-1500.
    • (2001) J. Neurosci , vol.21 , pp. 1490-1500
    • Needham, L.K.1    Thelen, K.2    Maness, P.F.3
  • 34
    • 0025027689 scopus 로고
    • Accumulation of N-CAM 180 at contact sites between neuroblastoma cells and latex beads coated with extracellular matrix molecules
    • Pollerberg, G. E., Nolte, C., and Schachner, M. (1990). Accumulation of N-CAM 180 at contact sites between neuroblastoma cells and latex beads coated with extracellular matrix molecules. Eur. J. Neurosci. 2, 879-887.
    • (1990) Eur. J. Neurosci , vol.2 , pp. 879-887
    • Pollerberg, G.E.1    Nolte, C.2    Schachner, M.3
  • 36
    • 0037456539 scopus 로고    scopus 로고
    • Two distinct mechanisms target membrane proteins to the axonal surface
    • Sampo, B., Kaech, S., Kunz, S., and Banker, G. (2003). Two distinct mechanisms target membrane proteins to the axonal surface. Neuron 37, 611-624.
    • (2003) Neuron , vol.37 , pp. 611-624
    • Sampo, B.1    Kaech, S.2    Kunz, S.3    Banker, G.4
  • 37
    • 17844364008 scopus 로고    scopus 로고
    • Maintenance of neuronal positions in organized ganglia by SAX-7, a Caenorhabditis elegans homologue of L1
    • Sasakura, H., Inada, H., Kuhara, A., Fusaoka, E., Takemoto, D., Takeuchi, K., and Mori, I. (2005). Maintenance of neuronal positions in organized ganglia by SAX-7, a Caenorhabditis elegans homologue of L1. EMBO J. 24, 1477-1488.
    • (2005) EMBO J , vol.24 , pp. 1477-1488
    • Sasakura, H.1    Inada, H.2    Kuhara, A.3    Fusaoka, E.4    Takemoto, D.5    Takeuchi, K.6    Mori, I.7
  • 39
    • 0035158040 scopus 로고    scopus 로고
    • Cell adhesion molecule L1 in folded (horseshoe) and extended conformations
    • Schurmann, G., Haspel, J., Grumet, M., and Erickson, H. P. (2001). Cell adhesion molecule L1 in folded (horseshoe) and extended conformations. Mol. Biol. Cell 12, 1765-1773.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1765-1773
    • Schurmann, G.1    Haspel, J.2    Grumet, M.3    Erickson, H.P.4
  • 40
    • 0025304790 scopus 로고
    • Concentration of membrane antigens by forward transport and trapping in neuronal growth cones
    • Sheetz, M. P., Baumrind, N. L., Wayne, D. B., and Pearlman, A. L. (1990). Concentration of membrane antigens by forward transport and trapping in neuronal growth cones. Cell 61, 231-241.
    • (1990) Cell , vol.61 , pp. 231-241
    • Sheetz, M.P.1    Baumrind, N.L.2    Wayne, D.B.3    Pearlman, A.L.4
  • 41
    • 0034717802 scopus 로고    scopus 로고
    • Plasmin-sensitive dibasic sequences in the third fibronectin-like domain of L1-cell adhesion molecule (CAM) facilitate homomultimerization and concomitant integrin recruitment
    • Silletti, S., Mei, F., Sheppard, D., and Montgomery, A. M. (2000). Plasmin-sensitive dibasic sequences in the third fibronectin-like domain of L1-cell adhesion molecule (CAM) facilitate homomultimerization and concomitant integrin recruitment. J. Cell Biol. 149, 1485-1502.
    • (2000) J. Cell Biol , vol.149 , pp. 1485-1502
    • Silletti, S.1    Mei, F.2    Sheppard, D.3    Montgomery, A.M.4
  • 42
    • 0032489869 scopus 로고    scopus 로고
    • The Ig superfamily cell adhesion molecule, apCAM, mediates growth cone steering by substrate-cytoskeletal coupling
    • Suter, D. M., Errante, L. D., Belotserkovsky, V., and Forscher, P. (1998). The Ig superfamily cell adhesion molecule, apCAM, mediates growth cone steering by substrate-cytoskeletal coupling. J. Cell Biol. 141, 227-240.
    • (1998) J. Cell Biol , vol.141 , pp. 227-240
    • Suter, D.M.1    Errante, L.D.2    Belotserkovsky, V.3    Forscher, P.4
  • 43
    • 0141737070 scopus 로고    scopus 로고
    • Direct imaging of lateral movements of AMPA receptors inside synapses
    • Tardin, C., Cognet, L., Bats, C., Lounis, B., and Choquet, D. (2003). Direct imaging of lateral movements of AMPA receptors inside synapses. EMBO J. 22, 4656-4665.
    • (2003) EMBO J , vol.22 , pp. 4656-4665
    • Tardin, C.1    Cognet, L.2    Bats, C.3    Lounis, B.4    Choquet, D.5
  • 44
    • 31944444653 scopus 로고    scopus 로고
    • Regulation of N-cadherin dynamics at neuronal contacts by ligand binding and cytoskeletal coupling
    • Thoumine, O., Lambert, M., Mege, R. M., and Choquet, D. (2006). Regulation of N-cadherin dynamics at neuronal contacts by ligand binding and cytoskeletal coupling. Mol. Biol. Cell 17, 862-875.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 862-875
    • Thoumine, O.1    Lambert, M.2    Mege, R.M.3    Choquet, D.4
  • 46
    • 33845885777 scopus 로고    scopus 로고
    • Attractive axon guidance involves asymmetric membrane transport and exocytosis in the growth cone
    • Tojima, T., Akiyama, H., Itofusa, R., Li, Y., Katayama, H., Miyawaki, A., and Kamiguchi, H. (2007). Attractive axon guidance involves asymmetric membrane transport and exocytosis in the growth cone. Nat. Neurosci. 10, 58-66.
    • (2007) Nat. Neurosci , vol.10 , pp. 58-66
    • Tojima, T.1    Akiyama, H.2    Itofusa, R.3    Li, Y.4    Katayama, H.5    Miyawaki, A.6    Kamiguchi, H.7
  • 47
    • 0030667933 scopus 로고    scopus 로고
    • The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation
    • Tuvia, S., Garver, T. D., and Bennett, V. (1997). The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation. Proc. Natl. Acad. Sci. USA 94, 12957-12962.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12957-12962
    • Tuvia, S.1    Garver, T.D.2    Bennett, V.3
  • 48
    • 33744764926 scopus 로고    scopus 로고
    • MAP kinase pathway-dependent phosphorylation of the L1-CAM ankyrin binding site regulates neuronal growth
    • Whittard, J. D., Sakurai, T., Cassella, M. R., Gazdoiu, M., and Felsenfeld, D. P. (2006). MAP kinase pathway-dependent phosphorylation of the L1-CAM ankyrin binding site regulates neuronal growth. Mol. Biol. Cell 17, 2696-2706.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2696-2706
    • Whittard, J.D.1    Sakurai, T.2    Cassella, M.R.3    Gazdoiu, M.4    Felsenfeld, D.P.5
  • 50
    • 0028841097 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule L1 is not required for homophilic adhesion
    • Wong, E. V., Cheng, G., Payne, H. R., and Lemmon, V. (1995). The cytoplasmic domain of the cell adhesion molecule L1 is not required for homophilic adhesion. Neurosci. Lett. 200, 155-158.
    • (1995) Neurosci. Lett , vol.200 , pp. 155-158
    • Wong, E.V.1    Cheng, G.2    Payne, H.R.3    Lemmon, V.4
  • 51
    • 0029800074 scopus 로고    scopus 로고
    • Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism
    • Xia, Z., Dudek, H., Miranti, C. K., and Greenberg, M. E. (1996). Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism. J. Neurosci. 16, 5425-5436.
    • (1996) J. Neurosci , vol.16 , pp. 5425-5436
    • Xia, Z.1    Dudek, H.2    Miranti, C.K.3    Greenberg, M.E.4
  • 52
    • 0030848953 scopus 로고    scopus 로고
    • Thrombin receptor on rat primary hippocampal neurons: Coupled calcium and cAMP responses
    • Yang, Y., Akiyama, H., Fenton, J. W., 2nd, and Brewer, G. J. (1997). Thrombin receptor on rat primary hippocampal neurons: coupled calcium and cAMP responses. Brain Res. 761, 11-18.
    • (1997) Brain Res , vol.761 , pp. 11-18
    • Yang, Y.1    Akiyama, H.2    Fenton 2nd, J.W.3    Brewer, G.J.4
  • 53
    • 0031843420 scopus 로고    scopus 로고
    • Identification of a homophilic binding site in immunoglobulin-like domain 2 of the cell adhesion molecule L1
    • Zhao, X., Yip, P. M., and Siu, C. H. (1998). Identification of a homophilic binding site in immunoglobulin-like domain 2 of the cell adhesion molecule L1. J. Neurochem. 71, 960-971.
    • (1998) J. Neurochem , vol.71 , pp. 960-971
    • Zhao, X.1    Yip, P.M.2    Siu, C.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.