메뉴 건너뛰기




Volumn 162, Issue 3, 2003, Pages 489-498

Local ERM activation and dynamic growth cones at schwann cell tips implicated in efficient formation of nodes of Ranvier

Author keywords

Glial cells; Growth cones; Microvilli; Myelin sheath; Nodes of Ranvier

Indexed keywords

EZRIN; MOESIN; RADIXIN; RHO KINASE; SODIUM PROTON EXCHANGE PROTEIN 3;

EID: 0042733242     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200303039     Document Type: Article
Times cited : (75)

References (39)
  • 1
    • 0034065232 scopus 로고    scopus 로고
    • On the molecular architecture of myelinated fibers
    • Arroyo, E.J., and S.S. Scherer. 2000. On the molecular architecture of myelinated fibers. Histochem. Cell Biol. 113:1-18.
    • (2000) Histochem. Cell Biol. , vol.113 , pp. 1-18
    • Arroyo, E.J.1    Scherer, S.S.2
  • 3
    • 0018381233 scopus 로고
    • Studies on cultured rat Schwann cells. I. Establishment of purified populations from cultures of peripheral nerve
    • Brockes, J.P., K.L. Fields, and M.C. Raff. 1979. Studies on cultured rat Schwann cells. I. Establishment of purified populations from cultures of peripheral nerve. Brain Res. 165:105-118.
    • (1979) Brain Res , vol.165 , pp. 105-118
    • Brockes, J.P.1    Fields, K.L.2    Raff, M.C.3
  • 4
    • 0033506221 scopus 로고    scopus 로고
    • Clustering of neuronal sodium channels requires contact with myelinating Schwann cells
    • Ching, W., G. Zanazzi, S.R. Levinson, and J.L. Salzer. 1999. Clustering of neuronal sodium channels requires contact with myelinating Schwann cells. J. Neurocytol. 28:295-301.
    • (1999) J. Neurocytol. , vol.28 , pp. 295-301
    • Ching, W.1    Zanazzi, G.2    Levinson, S.R.3    Salzer, J.L.4
  • 5
    • 0030443956 scopus 로고    scopus 로고
    • Molecular composition of the node of Ranvier: Identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments
    • Davis, J.Q., S. Lambert, and V. Bennett. 1996. Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments. J. Cell Biol. 135:1355-1367.
    • (1996) J. Cell Biol. , vol.135 , pp. 1355-1367
    • Davis, J.Q.1    Lambert, S.2    Bennett, V.3
  • 6
    • 0030904472 scopus 로고    scopus 로고
    • Clustering of voltage-sensitive sodium channels on axons is independent of direct Schwann cell contact in the dystrophic mouse
    • Deerinck, T.J., S.R. Levinson, G.V. Bennett, and M.H. Ellisman. 1997. Clustering of voltage-sensitive sodium channels on axons is independent of direct Schwann cell contact in the dystrophic mouse. J. Neurosci. 17:5080-5088.
    • (1997) J. Neurosci. , vol.17 , pp. 5080-5088
    • Deerinck, T.J.1    Levinson, S.R.2    Bennett, G.V.3    Ellisman, M.H.4
  • 7
    • 0023575754 scopus 로고
    • Differentiation of axon-related Schwann cells in vitro. I. Ascorbic acid regulates basal lamina assembly and myelin formation
    • Eldridge, C.F., M.B. Bunge, R.P. Bunge, and P.M. Wood. 1987. Differentiation of axon-related Schwann cells in vitro. I. Ascorbic acid regulates basal lamina assembly and myelin formation. J. Cell Biol. 105:1023-1034.
    • (1987) J. Cell Biol. , vol.105 , pp. 1023-1034
    • Eldridge, C.F.1    Bunge, M.B.2    Bunge, R.P.3    Wood, P.M.4
  • 8
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary, R., and A. Bretscher. 1995. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol. Biol. Cell. 6:1061-1075.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 9
    • 0032168919 scopus 로고    scopus 로고
    • A dicistronic retroviral vector and culture model for analysis of neuron-Schwann cell interactions
    • Howe, D.G., and K.D. McCarthy. 1998. A dicistronic retroviral vector and culture model for analysis of neuron-Schwann cell interactions. J. Neurosci. Methods. 83:133-142.
    • (1998) J. Neurosci. Methods , vol.83 , pp. 133-142
    • Howe, D.G.1    McCarthy, K.D.2
  • 10
    • 0025807797 scopus 로고
    • Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier
    • Ichimura, T., and M.H. Ellisman. 1991. Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier. J. Neurocytol. 20:667-681.
    • (1991) J. Neurocytol. , vol.20 , pp. 667-681
    • Ichimura, T.1    Ellisman, M.H.2
  • 12
    • 0028199794 scopus 로고
    • The Schwann cell precursor and its fate: A study of cell death and differentiation during gliogenesis in rat embryonic nerves
    • Jessen, K.R., A. Brennan, L. Morgan, R. Mirsky, A. Kent, Y. Hashimoto, and J. Gavrilovic. 1994. The Schwann cell precursor and its fate: a study of cell death and differentiation during gliogenesis in rat embryonic nerves. Neuron. 12:509-527.
    • (1994) Neuron , vol.12 , pp. 509-527
    • Jessen, K.R.1    Brennan, A.2    Morgan, L.3    Mirsky, R.4    Kent, A.5    Hashimoto, Y.6    Gavrilovic, J.7
  • 13
    • 0032603022 scopus 로고    scopus 로고
    • Regulation of cytoskeleton and cell adhesion by Rho targets
    • Kaibuchi, K. 1999. Regulation of cytoskeleton and cell adhesion by Rho targets. Prog. Mol. Subcell. Biol. 22:23-38.
    • (1999) Prog. Mol. Subcell. Biol. , vol.22 , pp. 23-38
    • Kaibuchi, K.1
  • 15
    • 0037148526 scopus 로고    scopus 로고
    • [β]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier
    • Komada, M., and P. Soriano. 2002. [β]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier. J. Cell Biol. 156:337-348.
    • (2002) J. Cell Biol. , vol.156 , pp. 337-348
    • Komada, M.1    Soriano, P.2
  • 16
    • 0025231649 scopus 로고
    • An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves
    • Kordeli, E., J. Davis, B. Trapp, and V. Bennett. 1990. An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves. J. Cell Biol. 110:1341-1352.
    • (1990) J. Cell Biol. , vol.110 , pp. 1341-1352
    • Kordeli, E.1    Davis, J.2    Trapp, B.3    Bennett, V.4
  • 17
    • 0028985712 scopus 로고
    • AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • Kordeli, E., S. Lambert, and V. Bennett. 1995. AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J. Biol. Chem. 270:2352-2359.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3
  • 18
    • 0030824001 scopus 로고    scopus 로고
    • Morphogenesis of the node of Ranvier: Co-clusters of ankyrin and ankyrin-binding integral proteins define early developmental intermediates
    • Lambert, S., J.Q. Davis, and V. Bennett. 1997. Morphogenesis of the node of Ranvier: co-clusters of ankyrin and ankyrin-binding integral proteins define early developmental intermediates. J. Neurosci. 17:7025-7036.
    • (1997) J. Neurosci. , vol.17 , pp. 7025-7036
    • Lambert, S.1    Davis, J.Q.2    Bennett, V.3
  • 19
    • 0035960734 scopus 로고    scopus 로고
    • Nr-CAM and neurofascin interactions regulate ankyrin G and sodium channel clustering at the node of Ranvier
    • Lustig, M., G. Zanazzi, T. Sakurai, C. Blanco, S.R. Levinson, S. Lambert, M. Grumet, and J.L. Salzer. 2001. Nr-CAM and neurofascin interactions regulate ankyrin G and sodium channel clustering at the node of Ranvier. Curr. Biol. 11:1864-1869.
    • (2001) Curr. Biol. , vol.11 , pp. 1864-1869
    • Lustig, M.1    Zanazzi, G.2    Sakurai, T.3    Blanco, C.4    Levinson, S.R.5    Lambert, S.6    Grumet, M.7    Salzer, J.L.8
  • 20
    • 0022976359 scopus 로고
    • Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve
    • Martini, R., and M. Schachner. 1986. Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve. J. Cell Biol. 103:2439-2448.
    • (1986) J. Cell Biol. , vol.103 , pp. 2439-2448
    • Martini, R.1    Schachner, M.2
  • 21
    • 0023895353 scopus 로고
    • Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and myelin-associated glycoprotein) in regenerating adult mouse sciatic nerve
    • Martini, R., and M. Schachner. 1988. Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and myelin-associated glycoprotein) in regenerating adult mouse sciatic nerve. J. Cell Biol. 106:1735-1746.
    • (1988) J. Cell Biol. , vol.106 , pp. 1735-1746
    • Martini, R.1    Schachner, M.2
  • 22
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui, T., M. Maeda, Y. Doi, S. Yonemura, M. Amano, K. Kaibuchi, and S. Tsukita. 1998. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140:647-657.
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7
  • 24
    • 0032547839 scopus 로고    scopus 로고
    • Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons
    • Paglini, G., P. Kunda, S. Quiroga, K. Kosik, and A. Caceres. 1998. Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons. J. Cell Biol. 143:443-455.
    • (1998) J. Cell Biol. , vol.143 , pp. 443-455
    • Paglini, G.1    Kunda, P.2    Quiroga, S.3    Kosik, K.4    Caceres, A.5
  • 25
    • 0034660093 scopus 로고    scopus 로고
    • Fluorescent myelin proteins provide new tools to study the myelination process
    • Pedraza, L., and D.R. Colman. 2000. Fluorescent myelin proteins provide new tools to study the myelination process. J. Neurosci. Res. 60:697-703.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 697-703
    • Pedraza, L.1    Colman, D.R.2
  • 26
    • 0032541057 scopus 로고    scopus 로고
    • The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
    • Reczek, D., and A. Bretscher. 1998. The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule. J. Biol. Chem. 273:18452-18458.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18452-18458
    • Reczek, D.1    Bretscher, A.2
  • 27
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • Reczek, D., M. Berryman, and A. Bretscher. 1997. Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J. Cell Biol. 139:169-179.
    • (1997) J. Cell Biol. , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 28
    • 0017342059 scopus 로고
    • Density of sodium channels in mammalian myelinated nerve fibers and nature of the axonal membrane under the myelin sheath
    • Ritchie, J.M., and R.B. Rogart. 1977. Density of sodium channels in mammalian myelinated nerve fibers and nature of the axonal membrane under the myelin sheath. Proc. Natl. Acad. Sci. USA. 74:211-215.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 211-215
    • Ritchie, J.M.1    Rogart, R.B.2
  • 29
    • 0036130074 scopus 로고    scopus 로고
    • Recent progress on the molecular organization of myelinated axons
    • Scherer, S.S., and E.J. Arroyo. 2002. Recent progress on the molecular organization of myelinated axons. J. Peripher. Nerv. Syst. 7:1-12.
    • (2002) J. Peripher. Nerv. Syst. , vol.7 , pp. 1-12
    • Scherer, S.S.1    Arroyo, E.J.2
  • 30
    • 0035879768 scopus 로고    scopus 로고
    • Ezrin, radixin, and moesin are components of Schwann cell microvilli
    • Scherer, S.S., T. Xu, P. Crino, E.J. Arroyo, and D.H. Gutmann. 2001. Ezrin, radixin, and moesin are components of Schwann cell microvilli. J. Neurosci. Res. 65:150-164.
    • (2001) J. Neurosci. Res. , vol.65 , pp. 150-164
    • Scherer, S.S.1    Xu, T.2    Crino, P.3    Arroyo, E.J.4    Gutmann, D.H.5
  • 31
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R.J., M. Henry, F. Solomon, and T. Jacks. 1998. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell. 9:403-419.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 32
    • 0034605041 scopus 로고    scopus 로고
    • CD44 enhances neuregulin signaling by Schwann cells
    • Sherman, L.S., T.A. Rizvi, S. Karyala, and N. Ratner. 2000. CD44 enhances neuregulin signaling by Schwann cells. J. Cell Biol. 150:1071-1084.
    • (2000) J. Cell Biol. , vol.150 , pp. 1071-1084
    • Sherman, L.S.1    Rizvi, T.A.2    Karyala, S.3    Ratner, N.4
  • 33
    • 0024539750 scopus 로고
    • Sodium channels in single demyelinated mammalian axons
    • Shrager, P. 1989. Sodium channels in single demyelinated mammalian axons. Brain Res. 483:149-154.
    • (1989) Brain Res. , vol.483 , pp. 149-154
    • Shrager, P.1
  • 34
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi, K., T. Sasaki, A. Mammoto, K. Takaishi, T. Kameyama, S. Tsukita, and Y. Takai. 1997. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272:23371-23375.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Takai, Y.7
  • 35
    • 0024521890 scopus 로고
    • Co-localization of the myelin-associated glycoprotein and the microfilament components, F-actin and spectrin, in Schwann cells of myelinated nerve fibres
    • Trapp, B.D., S.B. Andrews, A. Wong, M. O'Connell, and J.W. Griffin. 1989. Co-localization of the myelin-associated glycoprotein and the microfilament components, F-actin and spectrin, in Schwann cells of myelinated nerve fibres. J. Neurocytol. 18:47-60.
    • (1989) J. Neurocytol. , vol.18 , pp. 47-60
    • Trapp, B.D.1    Andrews, S.B.2    Wong, A.3    O'Connell, M.4    Griffin, J.W.5
  • 37
    • 0029781360 scopus 로고    scopus 로고
    • The clustering of axonal sodium channels during development of the peripheral nervous system
    • Vabnick, I., S.D. Novakovic, S.R. Levinson, M. Schachner, and P. Shrager. 1996. The clustering of axonal sodium channels during development of the peripheral nervous system. J. Neurosci. 16:4914-4922.
    • (1996) J. Neurosci. , vol.16 , pp. 4914-4922
    • Vabnick, I.1    Novakovic, S.D.2    Levinson, S.R.3    Schachner, M.4    Shrager, P.5
  • 38
    • 0035884770 scopus 로고    scopus 로고
    • Regulation of Schwann cell morphology and adhesion by receptor-mediated lysophosphatidic acid signaling
    • Weiner, J.A., N. Fukushima, J.J. Contos, S.S. Scherer, and J. Chun. 2001. Regulation of Schwann cell morphology and adhesion by receptor-mediated lysophosphatidic acid signaling. J. Neurosci. 21:7069-7078.
    • (2001) J. Neurosci. , vol.21 , pp. 7069-7078
    • Weiner, J.A.1    Fukushima, N.2    Contos, J.J.3    Scherer, S.S.4    Chun, J.5
  • 39
    • 0037096169 scopus 로고    scopus 로고
    • Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: An essential role for polyphosphoinositides in vivo
    • Yonemura, S., T. Matsui, and S. Tsukita. 2002. Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. J. Cell Sci. 115:2569-2580.
    • (2002) J. Cell Sci. , vol.115 , pp. 2569-2580
    • Yonemura, S.1    Matsui, T.2    Tsukita, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.