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Volumn 149, Issue 2, 2000, Pages 491-501

The glycosylphosphatidyl inositol-anchored adhesion molecule F3/contactin is required for surface transport of paranodin/contactin- associated protein (caspr)

Author keywords

GPI anchor; Lipid rafts; Myelination; Neurexin; Node of Ranvier

Indexed keywords

CONTACTIN; FIBRONECTIN; GLYCOSYLPHOSPHATIDYLINOSITOL; IMMUNOGLOBULIN; NERVE CELL ADHESION MOLECULE; NEUREXIN; TRITON X 100;

EID: 0034678437     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.149.2.491     Document Type: Article
Times cited : (117)

References (44)
  • 2
    • 0031720684 scopus 로고    scopus 로고
    • Neurexin IV, caspr and paranodin - Novel members of the neurexin family: Encounters of axons and glia
    • Bellen, H.J., Y. Lu, R. Beckstead, and M.A. Bhat. 1998. Neurexin IV, caspr and paranodin - novel members of the neurexin family: encounters of axons and glia. Trends Neurosci. 10:444-449.
    • (1998) Trends Neurosci. , vol.10 , pp. 444-449
    • Bellen, H.J.1    Lu, Y.2    Beckstead, R.3    Bhat, M.A.4
  • 4
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched subdomains during transport to the apical surface
    • Brown, D., and J. Rose. 1992. Sorting of GPI-anchored proteins to glycolipid-enriched subdomains during transport to the apical surface. Cell. 68:533-544.
    • (1992) Cell. , vol.68 , pp. 533-544
    • Brown, D.1    Rose, J.2
  • 5
    • 0030273292 scopus 로고    scopus 로고
    • Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamily
    • Brümmendorf, T., and F. Rathjen. 1996. Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamily. Curr. Opin. Neurobiol. 6:584-592.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 584-592
    • Brümmendorf, T.1    Rathjen, F.2
  • 6
    • 0027158056 scopus 로고
    • The axonal recognition molecule F11 is a multifunctional protein: Specific domains mediate interactions with Ng-CAM and restrictin
    • Brümmendorf, T., M. Hubert, U. Treubert, R. Leuschner, A. Tarnok, and F. Rathjen. 1993. The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictin. Neuron. 10:711-727.
    • (1993) Neuron. , vol.10 , pp. 711-727
    • Brümmendorf, T.1    Hubert, M.2    Treubert, U.3    Leuschner, R.4    Tarnok, A.5    Rathjen, F.6
  • 7
    • 0030200165 scopus 로고    scopus 로고
    • F3 neuronal adhesion molecule controls outgrowth and fasciculation of cerebellar granule cell neurites: A cell-type specific effect mediated by the Ig-like domains
    • Buttiglione, M., J.M. Revest, G. Rougon, and C. Faivre-Sarrailh. 1996. F3 neuronal adhesion molecule controls outgrowth and fasciculation of cerebellar granule cell neurites: a cell-type specific effect mediated by the Ig-like domains. Mol. Cell. Neurosci. 8:53-69.
    • (1996) Mol. Cell. Neurosci. , vol.8 , pp. 53-69
    • Buttiglione, M.1    Revest, J.M.2    Rougon, G.3    Faivre-Sarrailh, C.4
  • 8
    • 17344368338 scopus 로고    scopus 로고
    • A functional interaction between the neuronal adhesion molecules TAG-1 and F3 modulates neurite outgrowth and fasciculation of cerebellar granule cells
    • Buttiglione, M., J.M. Revest, O. Pavlou, D. Karagogeos, A. Furley, G. Rougon, and C. Faivre-Sarrailh. 1998. A functional interaction between the neuronal adhesion molecules TAG-1 and F3 modulates neurite outgrowth and fasciculation of cerebellar granule cells. J. Neurosci. 18:6853-6870.
    • (1998) J. Neurosci. , vol.18 , pp. 6853-6870
    • Buttiglione, M.1    Revest, J.M.2    Pavlou, O.3    Karagogeos, D.4    Furley, A.5    Rougon, G.6    Faivre-Sarrailh, C.7
  • 9
    • 0030012213 scopus 로고    scopus 로고
    • The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: Involvement of the FNIII repeats
    • Cervello, M., V. Matranga, P. Durbec, G. Rougon, and S. Gomez. 1996. The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: involvement of the FNIII repeats. J. Cell Sci. 109:699-704.
    • (1996) J. Cell Sci. , vol.109 , pp. 699-704
    • Cervello, M.1    Matranga, V.2    Durbec, P.3    Rougon, G.4    Gomez, S.5
  • 10
    • 0030443956 scopus 로고    scopus 로고
    • +/third FNIII domain ) and NrCAM at nodal axon segments
    • +/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
  • 11
    • 0033552610 scopus 로고    scopus 로고
    • Axo-glial interactions regulate the localization of axonal paranodal proteins
    • Dupree, J.L., J.A. Girault, and B. Popko. 1999. Axo-glial interactions regulate the localization of axonal paranodal proteins. J. Cell Biol. 147:1145-1152.
    • (1999) J. Cell Biol. , vol.147 , pp. 1145-1152
    • Dupree, J.L.1    Girault, J.A.2    Popko, B.3
  • 12
    • 0026718214 scopus 로고
    • A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth
    • Durbec, P., G. Gennarini, C. Goridis, and G. Rougon. 1992. A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth. J. Cell Biol. 117:877-887.
    • (1992) J. Cell Biol. , vol.117 , pp. 877-887
    • Durbec, P.1    Gennarini, G.2    Goridis, C.3    Rougon, G.4
  • 13
    • 0028351388 scopus 로고
    • Different domains of the F3 neuronal adhesion molecule are involved in adhesion and neurite outgrowth promotion
    • Durbec, P., G. Gennarini, M. Buttiglione, S. Gomez, and G. Rougon. 1994. Different domains of the F3 neuronal adhesion molecule are involved in adhesion and neurite outgrowth promotion. Eur. J. Neurosci. 6:461-472.
    • (1994) Eur. J. Neurosci. , vol.6 , pp. 461-472
    • Durbec, P.1    Gennarini, G.2    Buttiglione, M.3    Gomez, S.4    Rougon, G.5
  • 14
    • 0031453392 scopus 로고    scopus 로고
    • The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination
    • Einheber, S., G. Zanazzi, W. Ching, S. Scherer, T. Milner, E. Peles, and J. Salzer. 1997. The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination. J. Cell Biol. 139:1495-1506.
    • (1997) J. Cell Biol. , vol.139 , pp. 1495-1506
    • Einheber, S.1    Zanazzi, G.2    Ching, W.3    Scherer, S.4    Milner, T.5    Peles, E.6    Salzer, J.7
  • 15
    • 0030791189 scopus 로고    scopus 로고
    • Axonal molecules of the immunoglobulin superfamily bearing a GPI anchor: Their role in controlling neurite outgrowth
    • Faivre-Sarrailh, C., and G. Rougon. 1997. Axonal molecules of the immunoglobulin superfamily bearing a GPI anchor: their role in controlling neurite outgrowth. Mol. Cell. Neurosci. 9:109-115.
    • (1997) Mol. Cell. Neurosci. , vol.9 , pp. 109-115
    • Faivre-Sarrailh, C.1    Rougon, G.2
  • 16
    • 0025237057 scopus 로고
    • The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth promoting activity
    • Furley, A.J., S.B. Morton, D. Manalo, D. Karagogeos, J. Dodd, and T.M. Jessell. 1990. The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth promoting activity. Cell. 61:157-170.
    • (1990) Cell. , vol.61 , pp. 157-170
    • Furley, A.J.1    Morton, S.B.2    Manalo, D.3    Karagogeos, D.4    Dodd, J.5    Jessell, T.M.6
  • 17
    • 0025809906 scopus 로고
    • Transfected F3/F11 neuronal cell surface protein mediates intercellular adhesion and promotes neuntes outgrowth
    • Gennarini, G., P. Durbec, A. Boned, G. Rougon, and C. Goridis. 1991. Transfected F3/F11 neuronal cell surface protein mediates intercellular adhesion and promotes neuntes outgrowth. Neuron. 6:595-606.
    • (1991) Neuron , vol.6 , pp. 595-606
    • Gennarini, G.1    Durbec, P.2    Boned, A.3    Rougon, G.4    Goridis, C.5
  • 18
    • 0032425542 scopus 로고    scopus 로고
    • Janus kinases and focal adhesion kinases play in the 4.1 hand: A superfamily of band 4.1 domains important for cell structure and signal transduction
    • Girault, J.A., G. Labesse, J.P. Mornon, and I. Callebaut. 1998. Janus kinases and focal adhesion kinases play in the 4.1 hand: a superfamily of band 4.1 domains important for cell structure and signal transduction. Mol. Med. 4:751-769.
    • (1998) Mol. Med. , vol.4 , pp. 751-769
    • Girault, J.A.1    Labesse, G.2    Mornon, J.P.3    Callebaut, I.4
  • 19
  • 20
    • 0028972374 scopus 로고
    • Structure and function of the beta 2 subunit of brain sodium channels, a transmembrane glycoprotein with CAM motif
    • Isom, L.L., D.S. Ragsdale, K.S. De Jongh, R.E. Westenbroeck, B.F. Reber, T. Scheuer, and W.A. Catterall. 1995. Structure and function of the beta 2 subunit of brain sodium channels, a transmembrane glycoprotein with CAM motif. Cell. 83:433-442.
    • (1995) Cell. , vol.83 , pp. 433-442
    • Isom, L.L.1    Ragsdale, D.S.2    De Jongh, K.S.3    Westenbroeck, R.E.4    Reber, B.F.5    Scheuer, T.6    Catterall, W.A.7
  • 21
    • 15844365303 scopus 로고    scopus 로고
    • GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF
    • Jing, S., D. Wen, Y. Yu, P.L. Holst, Y. Luo, M. Fang, R. Tamir, L. Antonio, Z. Hu, R. Cupples, et al. 1996. GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF Cell. 85:1113-1124.
    • (1996) Cell. , vol.85 , pp. 1113-1124
    • Jing, S.1    Wen, D.2    Yu, Y.3    Holst, P.L.4    Luo, Y.5    Fang, M.6    Tamir, R.7    Antonio, L.8    Hu, Z.9    Cupples, R.10
  • 22
    • 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
  • 23
    • 0000441994 scopus 로고
    • Polarized apical distribution of glycosyl-phophatidylinositol-anchored proteins in a renal epithelial cell clone
    • Lisanti, M.P., M. Sargiacomo, L. Graeve, A. Saltiel, and E. Rodriguez-Boulan. 1989. Polarized apical distribution of glycosyl-phophatidylinositol-anchored proteins in a renal epithelial cell clone. Proc. Natl. Acad. Sci. USA. 85:9557-9561.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9557-9561
    • Lisanti, M.P.1    Sargiacomo, M.2    Graeve, L.3    Saltiel, A.4    Rodriguez-Boulan, E.5
  • 25
    • 0027723273 scopus 로고
    • Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/ Bravo
    • Morales, G., M. Hubert, T. Brümmendorf, U. Treubert, A. Tarnok, U. Schwarz, and F. Rathjen. 1993. Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/ Bravo. Neuron. 11:1113-1122.
    • (1993) Neuron. , vol.11 , pp. 1113-1122
    • Morales, G.1    Hubert, M.2    Brümmendorf, T.3    Treubert, U.4    Tarnok, A.5    Schwarz, U.6    Rathjen, F.7
  • 26
    • 0026327392 scopus 로고
    • An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes
    • Nabi, I.R., A. Le Bivic, D. Fambrough, and E. Rodriguez-Boulan. 1991. An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol. 115:1573-1584.
    • (1991) J. Cell Biol. , vol.115 , pp. 1573-1584
    • Nabi, I.R.1    Bivic, A.L.2    Fambrough, D.3    Rodriguez-Boulan, E.4
  • 27
    • 0029114404 scopus 로고
    • Characterization of functional domains of the tenascin-R (restrictin) polypeptide-cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R
    • Nörenberg, U., M. Hubert, T. Brümmendorf, A. Tarnok, and F.G. Rathjen. 1995. Characterization of functional domains of the tenascin-R (restrictin) polypeptide-cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R. J. Cell Biol. 130:473-484.
    • (1995) J. Cell Biol. , vol.130 , pp. 473-484
    • Nörenberg, U.1    Hubert, M.2    Brümmendorf, T.3    Tarnok, A.4    Rathjen, F.G.5
  • 28
    • 0028805468 scopus 로고
    • The F3 neuronal GPI-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn-kinase in cerebellum
    • Olive, S., C. Dubois, M. Schachner, and G. Rougon. 1995. The F3 neuronal GPI-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn-kinase in cerebellum. J. Neurochem. 65: 2307-2317.
    • (1995) J. Neurochem. , vol.65 , pp. 2307-2317
    • Olive, S.1    Dubois, C.2    Schachner, M.3    Rougon, G.4
  • 32
    • 0033000818 scopus 로고    scopus 로고
    • The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases z/β triggers bidirectional signalling between neurons and glial cells
    • Revest, J.M., C. Faivre-Sarrailh, N. Maeda, M. Noda, M. Schachner, and G. Rougon. 1999. The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases z/β triggers bidirectional signalling between neurons and glial cells. Eur. J. Neurosci. 11:1134-1147.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 1134-1147
    • Revest, J.M.1    Faivre-Sarrailh, C.2    Maeda, N.3    Noda, M.4    Schachner, M.5    Rougon, G.6
  • 33
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo, M., M. Sudol, T.I. Tang, and M. Lisanti. 1993. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122:789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, T.I.3    Lisanti, M.4
  • 34
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 35
  • 36
    • 0029852196 scopus 로고    scopus 로고
    • Neurofascin induces neuntes by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neurites
    • Volkmer, H., R. Leuschner, U. Zacharias, and F. Rathjen. 1996. Neurofascin induces neuntes by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neurites. J. Cell Biol. 135:1059-1069.
    • (1996) J. Cell Biol. , vol.135 , pp. 1059-1069
    • Volkmer, H.1    Leuschner, R.2    Zacharias, U.3    Rathjen, F.4
  • 37
    • 0032563627 scopus 로고    scopus 로고
    • Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells
    • Volkmer, H., U. Zacharias, U. Nörenberg, and F. Rathjen. 1998. Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells. J. Cell Biol. 142:1083-1093.
    • (1998) J. Cell Biol. , vol.142 , pp. 1083-1093
    • Volkmer, H.1    Zacharias, U.2    Nörenberg, U.3    Rathjen, F.4
  • 38
    • 0027424441 scopus 로고
    • Heteromultimeric K+ channels in terminal and juxta-paranodal regions of neurons
    • Wang, H., D.D. Hunkel, T.M. Martin, P.A. Schwartzkroin, and B.L. Tempel. 1993. Heteromultimeric K+ channels in terminal and juxta-paranodal regions of neurons. Nature. 365:75-79.
    • (1993) Nature , vol.365 , pp. 75-79
    • Wang, H.1    Hunkel, D.D.2    Martin, T.M.3    Schwartzkroin, P.A.4    Tempel, B.L.5
  • 39
    • 0027398432 scopus 로고
    • Molecular dissection of the myelinated axon
    • Waxman, S.G., and J.M. Ritchie. 1993. Molecular dissection of the myelinated axon. Ann. Neurol. 33:121-136.
    • (1993) Ann. Neurol. , vol.33 , pp. 121-136
    • Waxman, S.G.1    Ritchie, J.M.2
  • 40
    • 0029978087 scopus 로고    scopus 로고
    • Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11
    • Xiao, Z.C., J. Taylor, D. Montag, G. Rougon, and M. Schachner. 1996. Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11. Eur. J. Neurosci. 8:766-782.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 766-782
    • Xiao, Z.C.1    Taylor, J.2    Montag, D.3    Rougon, G.4    Schachner, M.5
  • 42
    • 0033605123 scopus 로고    scopus 로고
    • A glial-neuronal signaling pathway revealed by mutations in a neurexin-related protein
    • Yuan, L.L., and B. Ganetzky. 1999. A glial-neuronal signaling pathway revealed by mutations in a neurexin-related protein. Science. 283:1343-1345.
    • (1999) Science , vol.283 , pp. 1343-1345
    • Yuan, L.L.1    Ganetzky, B.2
  • 43
    • 0033571032 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase α (PTPα) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn
    • Zeng, L., L. D'alessandri, M.B. Kalousek, L. Vaughan, and C.J. Pallen. 1999. Protein tyrosine phosphatase α (PTPα) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn. J. Cell Biol. 147:707-713.
    • (1999) J. Cell Biol. , vol.147 , pp. 707-713
    • Zeng, L.1    D'alessandri, L.2    Kalousek, M.B.3    Vaughan, L.4    Pallen, C.J.5
  • 44
    • 0032555941 scopus 로고    scopus 로고
    • Restriction of 480/270-kD ankyrin G to axon proximal segments requires multiple ankyrin G-specific domains
    • Zhang, X., and V. Bennett. 1998. Restriction of 480/270-kD ankyrin G to axon proximal segments requires multiple ankyrin G-specific domains. J. Cell Biol. 142:1571-1581.
    • (1998) J. Cell Biol. , vol.142 , pp. 1571-1581
    • Zhang, X.1    Bennett, V.2


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