메뉴 건너뛰기




Volumn 22, Issue 3, 1999, Pages 511-524

EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CHOLESTEROL; EPHRIN B; GLUTAMATE RECEPTOR INTERACTING PROTEIN; LIGAND; PDZ ADAPTOR PROTEIN; PROTEIN TYROSINE KINASE; SPHINGOLIPID; UNCLASSIFIED DRUG;

EID: 0033103887     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80706-0     Document Type: Article
Times cited : (310)

References (54)
  • 1
    • 0033082959 scopus 로고    scopus 로고
    • Roles of ephrinB ligands and EphB receptors in cardiovascular development: Demarcation of arterial/venous domains, vascular morphogenesis and sprouting angiogenesis
    • Adams, R.H., Wilkinson, G.A., Weiss, C., Diella, F., Gale, N.W., Deutsch, U., Risau, W., and Klein, R. (1999). Roles of ephrinB ligands and EphB receptors in cardiovascular development: Demarcation of arterial/venous domains, vascular morphogenesis and sprouting angiogenesis. Genes Dev, 13, 295-306.
    • (1999) Genes Dev , vol.13 , pp. 295-306
    • Adams, R.H.1    Wilkinson, G.A.2    Weiss, C.3    Diella, F.4    Gale, N.W.5    Deutsch, U.6    Risau, W.7    Klein, R.8
  • 2
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison, D.W., Gelfand, V.I., Spector, I., and Craig, A.M. (1998). Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors. J. Neurosci. 18, 2423-2436.
    • (1998) J. Neurosci. , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 4
    • 0032576874 scopus 로고    scopus 로고
    • Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube
    • Bergemann, A.D., Zhang, L., Chiang, M.K., Brambilla, R., Klein, R., and Flanagan, J.G. (1998). Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. Oncogene 16, 471-480.
    • (1998) Oncogene , vol.16 , pp. 471-480
    • Bergemann, A.D.1    Zhang, L.2    Chiang, M.K.3    Brambilla, R.4    Klein, R.5    Flanagan, J.G.6
  • 5
    • 0032544535 scopus 로고    scopus 로고
    • Sorting out genes that regulate epithelial and neuronal polarity
    • Bredt, D.S. (1998). Sorting out genes that regulate epithelial and neuronal polarity. Cell 94, 691-694.
    • (1998) Cell , vol.94 , pp. 691-694
    • Bredt, D.S.1
  • 6
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown, D. (1993). The tyrosine kinase connection: How GPI-anchored proteins activate T cells. Curr. Opin. Immunol. 5, 349-354.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 349-354
    • Brown, D.1
  • 7
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D., and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.1    London, E.2
  • 8
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and Rose, J.K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 9
    • 0032103082 scopus 로고    scopus 로고
    • Signalling by Eph receptors and their ephrin ligands
    • Brückner, K., and Klein, R. (1998). Signalling by Eph receptors and their ephrin ligands. Curr. Opin. Neurobiol. 8, 375-382.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 375-382
    • Brückner, K.1    Klein, R.2
  • 10
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Brückner, K., Pasquale, E.B., and Klein, R. (1997). Tyrosine phosphorylation of transmembrane ligands for Eph receptors. Science 275, 1640-1643.
    • (1997) Science , vol.275 , pp. 1640-1643
    • Brückner, K.1    Pasquale, E.B.2    Klein, R.3
  • 11
    • 0030273552 scopus 로고    scopus 로고
    • + channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation
    • + channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation. Neuron 17, 759-767.
    • (1996) Neuron , vol.17 , pp. 759-767
    • Cohen, N.A.1    Brenman, J.E.2    Snyder, S.H.3    Bredt, D.S.4
  • 12
    • 0032524629 scopus 로고    scopus 로고
    • PDZ proteins organize synaptic signaling pathways
    • Craven, S.E., and Bredt, D.S. (1998). PDZ proteins organize synaptic signaling pathways. Cell 93, 495-498.
    • (1998) Cell , vol.93 , pp. 495-498
    • Craven, S.E.1    Bredt, D.S.2
  • 14
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong, H., O'Brien, R.J., Fung, E.T., Lanahan, A.A., Worley, P.F., and Huganir, R.L. (1997). GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386, 279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 16
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan, J.G., and Vanderhaeghen, P. (1998). The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci. 21, 309-345.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 17
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni, J.V., and Neel, B.G. (1993). Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 210, 179-187.
    • (1993) Anal. Biochem. , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 18
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson, T., and Kurzchalia, T.V. (1998). Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394, 802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 20
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., St. Jean, A., Woods, R.A., and Schiestl, R.H. (1992). Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20, 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 21
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P., and Simons, K. (1998). Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141, 929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 22
    • 0344816258 scopus 로고    scopus 로고
    • Nuk controls pathfinding of commissural axons in the mammalian central nervous system
    • Henkemeyer, M., Orioli, D., Henderson, J.T., Saxton, T.M., Roder, J., Pawson, T., and Klein, R. (1996). Nuk controls pathfinding of commissural axons in the mammalian central nervous system. Cell 86, 35-46.
    • (1996) Cell , vol.86 , pp. 35-46
    • Henkemeyer, M.1    Orioli, D.2    Henderson, J.T.3    Saxton, T.M.4    Roder, J.5    Pawson, T.6    Klein, R.7
  • 23
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman, C.S., and Winston, F. (1987). A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57, 267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 24
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signaling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S.J., Gale, N.W., Mbamalu, G., Yancopoulos, G.D., Henkemeyer, M., and Pawson, T. (1996). Bidirectional signaling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383, 722-725.
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1    Gale, N.W.2    Mbamalu, G.3    Yancopoulos, G.D.4    Henkemeyer, M.5    Pawson, T.6
  • 25
    • 0031947718 scopus 로고    scopus 로고
    • Cell-contact-dependent signaling in axon growth and guidance: Eph receptor tyrosine kinases and receptor protein tyrosine phosphatases β
    • Holland, S.J., Peles, E., Pawson, T., and Schlessinger, J. (1998). Cell-contact-dependent signaling in axon growth and guidance: Eph receptor tyrosine kinases and receptor protein tyrosine phosphatases β. Curr. Opin. Neurobiol. 8, 117-127.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 117-127
    • Holland, S.J.1    Peles, E.2    Pawson, T.3
  • 26
    • 0029977729 scopus 로고    scopus 로고
    • Antigen-mediated IgE receptor aggregation and signaling: A window on cell surface structure and dynamics
    • Holowka, D., and Baird, B. (1996). Antigen-mediated IgE receptor aggregation and signaling: A window on cell surface structure and dynamics. Annu. Rev. Biophys. Biomol. Struct. 25, 79-112.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 79-112
    • Holowka, D.1    Baird, B.2
  • 27
    • 0025948991 scopus 로고
    • Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to immobilon
    • Kamps, M. (1991). Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to immobilon. Methods Enzymol. 201, 21-27.
    • (1991) Methods Enzymol. , vol.201 , pp. 21-27
    • Kamps, M.1
  • 28
    • 0020634260 scopus 로고
    • Protein kinase C as a possible receptor protein of tumor-promoting phorbol esters
    • Kikkawa, U., Takai, Y., Tanaka, Y., Miyake, R., and Nishizuka, Y. (1983). Protein kinase C as a possible receptor protein of tumor-promoting phorbol esters. J. Biol. Chem. 258, 11442-11445.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11442-11445
    • Kikkawa, U.1    Takai, Y.2    Tanaka, Y.3    Miyake, R.4    Nishizuka, Y.5
  • 29
    • 0030720016 scopus 로고    scopus 로고
    • Polarized signaling: Basolateral receptor localization in epithelial cells by PDZ-containing proteins
    • Kim, S.K. (1997). Polarized signaling: Basolateral receptor localization in epithelial cells by PDZ-containing proteins. Curr. Opin. Cell Biol. 9, 853-859.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 853-859
    • Kim, S.K.1
  • 30
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.-C., Schenker, L.T., Kennedy, M.B., and Seeburg, P.H. (1995). Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269, 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.-C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 31
    • 0030744829 scopus 로고    scopus 로고
    • Interactions of ion channels and receptors with PDZ domain proteins
    • Kornau, H.-C., Seeburg, P.M., and Kennedy, M.B. (1997). Interactions of ion channels and receptors with PDZ domain proteins. Curr. Opin. Neurobiol. 7, 368-373.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 368-373
    • Kornau, H.-C.1    Seeburg, P.M.2    Kennedy, M.B.3
  • 32
    • 0030962317 scopus 로고    scopus 로고
    • The amino-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling
    • Labrador, J.P., Brambilla, R., and Klein, R. (1997). The amino-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling. EMBO J. 16, 3889-3897.
    • (1997) EMBO J. , vol.16 , pp. 3889-3897
    • Labrador, J.P.1    Brambilla, R.2    Klein, R.3
  • 34
    • 0030929986 scopus 로고    scopus 로고
    • The Eph receptor family: Axonal guidance by contact repulsion
    • Orioli, D., and Klein, R. (1997). The Eph receptor family: Axonal guidance by contact repulsion. Trends Genet. 13, 354-359.
    • (1997) Trends Genet. , vol.13 , pp. 354-359
    • Orioli, D.1    Klein, R.2
  • 35
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and Scott, J.D. (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 36
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signaling molecules to sub-membranous sites
    • Ponting, C.P., Phillips, C., Davies, K.E., and Blake, D.J. (1997). PDZ domains: Targeting signaling molecules to sub-membranous sites. Bioessays 19, 469-479.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 37
    • 0031460029 scopus 로고    scopus 로고
    • PDZ domain proteins: Scaffolds for signaling complexes
    • Ranganathan, R., and Ross, E.M. (1997). PDZ domain proteins: Scaffolds for signaling complexes. Curr. Biol. 7, R770-R773.
    • (1997) Curr. Biol. , vol.7
    • Ranganathan, R.1    Ross, E.M.2
  • 38
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., Roth, M.G., and Simons, K. (1997). Interaction of influenza virus haemagglutinin sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16, 5501-5508.
    • (1997) EMBO J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 39
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: Rounding up the latest suspects
    • Sheng, M. (1996). PDZs and receptor/channel clustering: Rounding up the latest suspects. Neuron 17, 575-578.
    • (1996) Neuron , vol.17 , pp. 575-578
    • Sheng, M.1
  • 40
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997). Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 43
    • 0028898641 scopus 로고
    • PICK1: A perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system
    • Staudinger, J., Zhou, J., Burgess, R., Elledge, S.J., and Olson, E.N. (1995). PICK1: A perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system. J. Cell Biol. 128, 263-271.
    • (1995) J. Cell Biol. , vol.128 , pp. 263-271
    • Staudinger, J.1    Zhou, J.2    Burgess, R.3    Elledge, S.J.4    Olson, E.N.5
  • 44
    • 0031465589 scopus 로고    scopus 로고
    • Specific interaction of the PDZ domain protein PICK1 with the COOH terminus of protein kinase C-alpha
    • Staudinger, J., Lu, J., and Olson, E.N. (1997). Specific interaction of the PDZ domain protein PICK1 with the COOH terminus of protein kinase C-alpha. J. Biol. Chem. 272, 32019-32024.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32019-32024
    • Staudinger, J.1    Lu, J.2    Olson, E.N.3
  • 45
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer, T.P., and Meyer, T. (1997). Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol. 139, 1447-1454.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 46
    • 0032031705 scopus 로고    scopus 로고
    • Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses
    • Stein, E., Lane, A.A., Cerretti, D.P., Schoecklmann, H.O., Schroff, A.D., Van Etten, R.L., and Daniel, T.O. (1998). Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev. 12, 667-678.
    • (1998) Genes Dev. , vol.12 , pp. 667-678
    • Stein, E.1    Lane, A.A.2    Cerretti, D.P.3    Schoecklmann, H.O.4    Schroff, A.D.5    Van Etten, R.L.6    Daniel, T.O.7
  • 48
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade
    • Tsunoda, S., Sierralta, J., Sun, Y., Bodner, R., Suzuki, E., Backer, A., Socolich, M., and Zuker, C.S. (1997). A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade. Nature 388, 243-249.
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.3    Bodner, R.4    Suzuki, E.5    Backer, A.6    Socolich, M.7    Zuker, C.S.8
  • 50
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and Mayor, S. (1998). GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394, 798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 51
    • 0032577446 scopus 로고    scopus 로고
    • Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4
    • Wang, H.U., Chen, Z.-F., and Anderson, D.J. (1998). Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell 93, 741-753.
    • (1998) Cell , vol.93 , pp. 741-753
    • Wang, H.U.1    Chen, Z.-F.2    Anderson, D.J.3
  • 52
    • 0001847685 scopus 로고
    • 35S-labelled oligonucleotide probes
    • W. Wisden and B.J. Morris, eds. (Oxford: Academic Press)
    • 35S-labelled oligonucleotide probes. In In Situ Hybridization Protocols for the Brain, W. Wisden and B.J. Morris, eds. (Oxford: Academic Press), 9-34.
    • (1994) In Situ Hybridization Protocols for the Brain , pp. 9-34
    • Wisden, W.1    Morris, B.J.2
  • 53
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C., and Seed, B. (1998). Membrane compartmentation is required for efficient T cell activation. Immunity 8, 723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 54
    • 0032577571 scopus 로고    scopus 로고
    • Vasculogenesis, angiogenesis, and growth factors: Ephrins enter the fray at the border
    • Yancopoulos, G.D., Klagsbrun, M., and Folkman, J. (1998). Vasculogenesis, angiogenesis, and growth factors: Ephrins enter the fray at the border. Cell 93, 661-664.
    • (1998) Cell , vol.93 , pp. 661-664
    • Yancopoulos, G.D.1    Klagsbrun, M.2    Folkman, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.