메뉴 건너뛰기




Volumn 85, Issue 4, 1996, Pages 513-523

Agrin acts via a MuSK receptor complex

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; PROTEIN TYROSINE KINASE;

EID: 15844380040     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81252-0     Document Type: Article
Times cited : (597)

References (49)
  • 1
    • 0029155684 scopus 로고
    • Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein complex
    • Apel, E.D., Roberds, S.L., Campbell, K.P., and Merlie, J.P. (1995). Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein complex. Neuron 15, 115-126.
    • (1995) Neuron , vol.15 , pp. 115-126
    • Apel, E.D.1    Roberds, S.L.2    Campbell, K.P.3    Merlie, J.P.4
  • 2
    • 0027165364 scopus 로고
    • Nerve growth factor: A tale of two receptors
    • Barbacid, M. (1993). Nerve growth factor: a tale of two receptors. Oncogene 8, 2033-2042.
    • (1993) Oncogene , vol.8 , pp. 2033-2042
    • Barbacid, M.1
  • 3
    • 0028914466 scopus 로고
    • The role of agrin in synapse formation
    • Bowe, M.A., and Fallon, J.R. (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
  • 4
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: A heteromeric complex related to dystroglycans
    • Bowe, M.A., Deyst, K.A., Leszyk, J.D., and Fallon, J.R. (1994). Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to dystroglycans. Neuron 12, 1173-1180.
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.A.1    Deyst, K.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 6
    • 0028306787 scopus 로고
    • A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering
    • Campanelli, J.T., Roberds, S.L., Campbell, K.P., and Scheller, R.H. (1994). A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering. Cell 77, 663-674.
    • (1994) Cell , vol.77 , pp. 663-674
    • Campanelli, J.T.1    Roberds, S.L.2    Campbell, K.P.3    Scheller, R.H.4
  • 7
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell, K.P. (1995). Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 80, 675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 8
    • 0027320024 scopus 로고
    • LIFRβ and gp130as heterodimerizing signal transducers of the tripartite CNTF receptor
    • Davis, S., Aldrich, T.H., Stahl, N., Taga, T., Kishimoto, T., Ip, N.Y., and Yancopoulos, G.D. (1993). LIFRβ and gp130as heterodimerizing signal transducers of the tripartite CNTF receptor. Science 260, 1805-1808.
    • (1993) Science , vol.260 , pp. 1805-1808
    • Davis, S.1    Aldrich, T.H.2    Stahl, N.3    Taga, T.4    Kishimoto, T.5    Ip, N.Y.6    Yancopoulos, G.D.7
  • 9
    • 0028110068 scopus 로고
    • Ligands for the EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity
    • Davis, S., Gale, N.W., Aldrich, T.H., Maisonpierre, P.C., Lhotak, V., Pawson, T., Goldfarb, M., and Yancopoulos, G.D. (1994). Ligands for the EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. Science 266, 816-819.
    • (1994) Science , vol.266 , pp. 816-819
    • Davis, S.1    Gale, N.W.2    Aldrich, T.H.3    Maisonpierre, P.C.4    Lhotak, V.5    Pawson, T.6    Goldfarb, M.7    Yancopoulos, G.D.8
  • 11
    • 0026634815 scopus 로고
    • The neurotrophins BDNF, NT-3, and NGF display distinct patterns of retrograde axonal transport in peripheral and central neurons
    • DiStefano, P.S., Friedman, B., Radziejewski, C., Alexander, C., Boland, P., Schick, C.M., Lindsay, R.M., and Weigand, S.J. (1992). The neurotrophins BDNF, NT-3, and NGF display distinct patterns of retrograde axonal transport in peripheral and central neurons. Neuron 8, 983-993.
    • (1992) Neuron , vol.8 , pp. 983-993
    • DiStefano, P.S.1    Friedman, B.2    Radziejewski, C.3    Alexander, C.4    Boland, P.5    Schick, C.M.6    Lindsay, R.M.7    Weigand, S.J.8
  • 12
    • 0002747447 scopus 로고
    • A non-label technology for real time biospecific interaction analysis
    • Fagerstam, L. (1991). A non-label technology for real time biospecific interaction analysis. Tech. Protein Chem. 2, 65-71.
    • (1991) Tech. Protein Chem. , vol.2 , pp. 65-71
    • Fagerstam, L.1
  • 13
    • 0028088813 scopus 로고
    • Building synapses: Agrin and dystroglycan stick together
    • Fallon, J.R., and Hall, Z.W. (1994). Building synapses: agrin and dystroglycan stick together. Trends Neurosci. 17, 469-473.
    • (1994) Trends Neurosci. , vol.17 , pp. 469-473
    • Fallon, J.R.1    Hall, Z.W.2
  • 14
    • 0026652948 scopus 로고
    • RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes
    • Ferns, M., Hoch, W., Camapnelli, J.T., Rupp, F., Hall, Z.W., and Scheller, R.H. (1992). RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes. Neuron 8, 1079-1086.
    • (1992) Neuron , vol.8 , pp. 1079-1086
    • Ferns, M.1    Hoch, W.2    Camapnelli, J.T.3    Rupp, F.4    Hall, Z.W.5    Scheller, R.H.6
  • 15
    • 0027517961 scopus 로고
    • The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans
    • Ferns, M., Campanelli, J.T., Hoch, W., Scheller, R.H., and Hall, Z.W. (1993). The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron 11, 491-502.
    • (1993) Neuron , vol.11 , pp. 491-502
    • Ferns, M.1    Campanelli, J.T.2    Hoch, W.3    Scheller, R.H.4    Hall, Z.W.5
  • 16
    • 0029928633 scopus 로고    scopus 로고
    • Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation
    • Ferns, M., Deiner, M., and Hall, Z. (1996). Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation. J. Cell Biol. 132, 937-944.
    • (1996) J. Cell Biol. , vol.132 , pp. 937-944
    • Ferns, M.1    Deiner, M.2    Hall, Z.3
  • 17
    • 0029050847 scopus 로고
    • Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice
    • Gautam, M., Noakes, P.G., Mudd, J., Nichol, M., Chu, G.C., Sanes, J.R., and Merlie, J.P. (1995). Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice. Nature 377, 232-236.
    • (1995) Nature , vol.377 , pp. 232-236
    • Gautam, M.1    Noakes, P.G.2    Mudd, J.3    Nichol, M.4    Chu, G.C.5    Sanes, J.R.6    Merlie, J.P.7
  • 19
    • 0028178082 scopus 로고
    • Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • Gee, S.H., Montanaro, F., Lindenbaum, M.H., and Carbonetto, S. (1994). Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 77, 675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 20
    • 0027177678 scopus 로고
    • The neurotrophins and their receptors
    • Glass, D.J., and Yancopoulos, G.D. (1993). The neurotrophins and their receptors. Trends Cell Biol. 3, 262-268.
    • (1993) Trends Cell Biol. , vol.3 , pp. 262-268
    • Glass, D.J.1    Yancopoulos, G.D.2
  • 21
    • 0025896342 scopus 로고
    • TrkB mediates BDNF/ NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor
    • Glass, D.J., Nye, S.H., Hantzopoulos, P., Macchi, M.J., Squinto, S.P., Goldfarb, M., and Yancopoulos, G.D. (1991). TrkB mediates BDNF/ NT-3-dependent survival and proliferation in fibroblasts lacking the low affinity NGF receptor. Cell 66, 405-413.
    • (1991) Cell , vol.66 , pp. 405-413
    • Glass, D.J.1    Nye, S.H.2    Hantzopoulos, P.3    Macchi, M.J.4    Squinto, S.P.5    Goldfarb, M.6    Yancopoulos, G.D.7
  • 22
    • 0021234220 scopus 로고
    • Components of Torpedo electric organ and muscle that cause aggregation of acetylcholine receptors on cultured muscle cells
    • Godfrey, E.W., Nitkin, R.M., Wallace, B.G., Rubin, L.L., and McMahan, U.J. (1984). Components of Torpedo electric organ and muscle that cause aggregation of acetylcholine receptors on cultured muscle cells. J. Cell Biol. 99, 615-627.
    • (1984) J. Cell Biol. , vol.99 , pp. 615-627
    • Godfrey, E.W.1    Nitkin, R.M.2    Wallace, B.G.3    Rubin, L.L.4    McMahan, U.J.5
  • 23
    • 0025492514 scopus 로고
    • The fibroblast growth factor family
    • Goldfarb, M. (1990). The fibroblast growth factor family. Cell Growth Differ. 1, 439-445.
    • (1990) Cell Growth Differ. , vol.1 , pp. 439-445
    • Goldfarb, M.1
  • 24
    • 0027480289 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall, Z.W., and Sanes, J.R. (1993). Synaptic structure and development: the neuromuscular junction. Cell 77/Neuron 10 (Suppl.), 99-121.
    • (1993) Cell 77/Neuron , vol.10 , Issue.SUPPL. , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 25
    • 0027369903 scopus 로고
    • Developmental regulation of highly active alternatively spliced forms of agrin
    • Hoch, W., Ferns, M., Campanelli, J.T., Hall, Z.W., and Scheller, R.H. (1993). Developmental regulation of highly active alternatively spliced forms of agrin. Neuron 11, 479-490.
    • (1993) Neuron , vol.11 , pp. 479-490
    • Hoch, W.1    Ferns, M.2    Campanelli, J.T.3    Hall, Z.W.4    Scheller, R.H.5
  • 26
    • 0028223672 scopus 로고
    • Structural domains of agrin required for clustering of nicotinic acetylcholine receptors
    • Hoch, W., Campanelli, J.T., Harrison, S., and Scheller, R.H. (1994). Structural domains of agrin required for clustering of nicotinic acetylcholine receptors. EMBO J. 13, 2814-2821.
    • (1994) EMBO J. , vol.13 , pp. 2814-2821
    • Hoch, W.1    Campanelli, J.T.2    Harrison, S.3    Scheller, R.H.4
  • 28
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., Lofas, S., and Lindquist, G. (1991). Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198, 268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Lofas, S.2    Lindquist, G.3
  • 29
    • 0027528768 scopus 로고
    • Similarities and differences in the way neurotrophins interact with the Trks in neuronal and nonneuronal cells
    • Ip, N.Y., Stitt, T.N., Tapley, P., Klein, R., Glass, D.J., Fandl, J., Greene, L.A., Barbacid, M., and Yancopoulos, G.D. (1993). Similarities and differences in the way neurotrophins interact with the Trks in neuronal and nonneuronal cells. Neuron 10, 137-149.
    • (1993) Neuron , vol.10 , pp. 137-149
    • Ip, N.Y.1    Stitt, T.N.2    Tapley, P.3    Klein, R.4    Glass, D.J.5    Fandl, J.6    Greene, L.A.7    Barbacid, M.8    Yancopoulos, G.D.9
  • 30
    • 0025797396 scopus 로고
    • Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF
    • Kaplan, D.R., Martin-Zanca, D., and Parada, L. (1991). Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF. Nature 350, 158-160.
    • (1991) Nature , vol.350 , pp. 158-160
    • Kaplan, D.R.1    Martin-Zanca, D.2    Parada, L.3
  • 31
    • 0028935085 scopus 로고
    • Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors
    • Martin, P.T., and Sanes, J.R. (1995). Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors. Neuron 14, 743-754.
    • (1995) Neuron , vol.14 , pp. 743-754
    • Martin, P.T.1    Sanes, J.R.2
  • 33
    • 0027467701 scopus 로고
    • 43K protein and acetylcholine receptors colocalize during the initial stages of neuromuscular synapse formation in vivo
    • Noakes, P.G., Phillips, W.D., Hanley, T.A., Sanes, J.R., and Merlie, J.P. (1993). 43K protein and acetylcholine receptors colocalize during the initial stages of neuromuscular synapse formation in vivo. Dev. Biol. 155, 275-280.
    • (1993) Dev. Biol. , vol.155 , pp. 275-280
    • Noakes, P.G.1    Phillips, W.D.2    Hanley, T.A.3    Sanes, J.R.4    Merlie, J.P.5
  • 34
    • 0026083114 scopus 로고
    • Induction of synaptic development in cultured muscle cells by basic fibroblast growth factor
    • Peng, H.B., Baker, L.P., and Chen, Q. (1991). Induction of synaptic development in cultured muscle cells by basic fibroblast growth factor. Neuron 6, 237-246.
    • (1991) Neuron , vol.6 , pp. 237-246
    • Peng, H.B.1    Baker, L.P.2    Chen, Q.3
  • 35
    • 0028052235 scopus 로고
    • Comparison of innervation and agrin-induced tyrosine phosphorylation of the nicotinic acetylcholine receptor
    • Qu, Z., and Huganir, R.L. (1994). Comparison of innervation and agrin-induced tyrosine phosphorylation of the nicotinic acetylcholine receptor. J. Neurosci. 14, 6834-6841.
    • (1994) J. Neurosci. , vol.14 , pp. 6834-6841
    • Qu, Z.1    Huganir, R.L.2
  • 36
    • 0026633248 scopus 로고
    • Agrin released by motor neurons induces the aggregation of acetylcholine receptors at neuromuscular junctions
    • Reist, N.E., Werle, M.J., and McMahan, U.J. (1992). Agrin released by motor neurons induces the aggregation of acetylcholine receptors at neuromuscular junctions. Neuron 8, 865-868.
    • (1992) Neuron , vol.8 , pp. 865-868
    • Reist, N.E.1    Werle, M.J.2    McMahan, U.J.3
  • 37
    • 0026583243 scopus 로고
    • The agrin gene encodes for a family of basal lamina proteins that differ in function and distribution
    • Ruegg, M.A., Tsim, K.W.K., Horton, S.E., Kroger, S., Escher, G., Gensch, E.M., and McMahan, U.J. (1992). The agrin gene encodes for a family of basal lamina proteins that differ in function and distribution. Neuron 8, 691-699.
    • (1992) Neuron , vol.8 , pp. 691-699
    • Ruegg, M.A.1    Tsim, K.W.K.2    Horton, S.E.3    Kroger, S.4    Escher, G.5    Gensch, E.M.6    McMahan, U.J.7
  • 39
    • 0026793456 scopus 로고
    • Growth factor signaling by receptor tyrosine kinases
    • Schlessinger, J., and Ullrich, A. (1992). Growth factor signaling by receptor tyrosine kinases. Neuron 9, 383-391.
    • (1992) Neuron , vol.9 , pp. 383-391
    • Schlessinger, J.1    Ullrich, A.2
  • 40
    • 0028338454 scopus 로고
    • Dystrophin-associated proteins and synapse formation: Is α-dystroglycan the agrin receptor?
    • Sealock, R., and Froehner, S.C. (1994). Dystrophin-associated proteins and synapse formation: is α-dystroglycan the agrin receptor? Cell 77, 617-619.
    • (1994) Cell , vol.77 , pp. 617-619
    • Sealock, R.1    Froehner, S.C.2
  • 41
    • 0027328343 scopus 로고
    • The alphas, betas, and kinases of cytokine receptor complexes
    • Stahl, N., and Yancopoulos, G.D. (1993). The alphas, betas, and kinases of cytokine receptor complexes. Cell 74, 587-590.
    • (1993) Cell , vol.74 , pp. 587-590
    • Stahl, N.1    Yancopoulos, G.D.2
  • 43
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • Sugiyama, J., Bowen, D.C., and Hall, Z.W. (1994). Dystroglycan binds nerve and muscle agrin. Neuron 13, 103-115.
    • (1994) Neuron , vol.13 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3
  • 46
    • 0024564197 scopus 로고
    • Agrin-induced specializations contain cytoplasmic, membrane, and extracellular matrix-associated components of the postsynaptic apparatus
    • Wallace, B.G. (1989). Agrin-induced specializations contain cytoplasmic, membrane, and extracellular matrix-associated components of the postsynaptic apparatus. J. Neurosci. 9, 1294-1302.
    • (1989) J. Neurosci. , vol.9 , pp. 1294-1302
    • Wallace, B.G.1
  • 47
    • 0028260234 scopus 로고
    • Staurosporine inhibits agrin-induced acetylcholine receptor phosphorylation and aggregation
    • Wallace, B.G. (1994). Staurosporine inhibits agrin-induced acetylcholine receptor phosphorylation and aggregation. J. Cell Biol. 125, 661-668.
    • (1994) J. Cell Biol. , vol.125 , pp. 661-668
    • Wallace, B.G.1
  • 48
    • 0028956758 scopus 로고
    • Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase
    • Wallace, B.G. (1995). Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase. J. Cell Biol. 128, 1121-1129.
    • (1995) J. Cell Biol. , vol.128 , pp. 1121-1129
    • Wallace, B.G.1
  • 49
    • 0025779156 scopus 로고
    • Agrin induces phosphorylation of the nicotinic acetylcholine receptor
    • Wallace, B.G., Qu, Z., and Huganir, R.L. (1991). Agrin induces phosphorylation of the nicotinic acetylcholine receptor. Neuron 6, 869-878.
    • (1991) Neuron , vol.6 , pp. 869-878
    • Wallace, B.G.1    Qu, Z.2    Huganir, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.