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Volumn 179, Issue 8, 2007, Pages 5159-5168

Inhibition of T cell activation by cyclic adenosine 5′-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein Ezrin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; APC PROTEIN; BINDING PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE 1; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; EZRIN; EZRIN BINDING PROTEIN 50; GLYCOSPHINGOLIPID; INTERLEUKIN 2; MULTIPROTEIN COMPLEX; PHOSPHOPROTEIN; PROTEIN TYROSINE KINASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; ACTIN; CYCLIC AMP; CYTOSKELETON PROTEIN; IMMUNOSUPPRESSIVE AGENT; LYMPHOCYTE ANTIGEN RECEPTOR; SODIUM HYDROGEN EXCHANGER REGULATORY FACTOR; SODIUM PROTON EXCHANGE PROTEIN; SODIUM-HYDROGEN EXCHANGER REGULATORY FACTOR;

EID: 38449120815     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.179.8.5159     Document Type: Article
Times cited : (106)

References (63)
  • 1
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken, K., and E. M. Aandahl. 2004. Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol. Rev. 84: 137-167.
    • (2004) Physiol. Rev , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 3
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • Wong, W., and J. D. Scott. 2004. AKAP signalling complexes: focal points in space and time. Nat. Rev. Mol. Cell Biol. 5: 959-970.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 4
    • 0028328869 scopus 로고
    • Location of cAMP-dependent protein kinase type I with the TCR-CD3 complex
    • Skalhegg, B. S., K. Tasken, V. Hansson, H. S. Huitfeldt, T. Jahnsen, and T. Lea. 1994. Location of cAMP-dependent protein kinase type I with the TCR-CD3 complex. Science 263: 84-87.
    • (1994) Science , vol.263 , pp. 84-87
    • Skalhegg, B.S.1    Tasken, K.2    Hansson, V.3    Huitfeldt, H.S.4    Jahnsen, T.5    Lea, T.6
  • 5
    • 0035910759 scopus 로고    scopus 로고
    • Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor
    • Vang, T., K. M. Torgersen, V. Sundvold, M. Saxena, F. O. Levy, B. S. Skalhegg, V. Hansson, T. Mustelin, and K. Tasken. 2001. Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor. J. Exp. Med. 193: 497-507.
    • (2001) J. Exp. Med , vol.193 , pp. 497-507
    • Vang, T.1    Torgersen, K.M.2    Sundvold, V.3    Saxena, M.4    Levy, F.O.5    Skalhegg, B.S.6    Hansson, V.7    Mustelin, T.8    Tasken, K.9
  • 6
    • 0028229539 scopus 로고
    • Erm family members as molecular linkers between the cell-surface glycoprotein Cd44 and actin-based cytoskeletons
    • Tsukita, S., K. Oishi, N. Sato, J. Sagara, A. Kawai, and S. Tsukita. 1994. Erm family members as molecular linkers between the cell-surface glycoprotein Cd44 and actin-based cytoskeletons. J. Cell Biol. 126: 391-401.
    • (1994) J. Cell Biol , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 7
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/Radixin/Moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura, S., M. Hirao, Y. Doi, N. Takahashi, T. Kondo, S. Tsukita, and S. Tsukita. 1998. Ezrin/Radixin/Moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J. Cell Biol. 140: 885-895.
    • (1998) J. Cell Biol , vol.140 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6    Tsukita, S.7
  • 9
    • 0035167035 scopus 로고    scopus 로고
    • Layilin, a novel integral membrane protein, is a hyaluronan receptor
    • Bono, P., K. Rubin, J. M. G. Higgins, and R. O. Hynes. 2001. Layilin, a novel integral membrane protein, is a hyaluronan receptor. Mol. Biol. Cell 12: 891-900.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 891-900
    • Bono, P.1    Rubin, K.2    Higgins, J.M.G.3    Hynes, R.O.4
  • 10
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2): Regulation by phosphatidylinositol 4, 5-bisphosphate
    • Heiska, L., K. Alfthan, M. Gronholm, P. Vilja, A. Vaheri, and O. Carpen. 1998. Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2): regulation by phosphatidylinositol 4, 5-bisphosphate. J. Biol. Chem. 273: 21893-21900.
    • (1998) J. Biol. Chem , vol.273 , pp. 21893-21900
    • Heiska, L.1    Alfthan, K.2    Gronholm, M.3    Vilja, P.4    Vaheri, A.5    Carpen, O.6
  • 11
    • 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, 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    Tsukita, S.7    Takai, Y.8
  • 13
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher, A., K. Edwards, and R. G. Fehon. 2002. ERM proteins and merlin: integrators at the cell cortex. Nat. Rev. Mol. Cell Biol. 3: 586-599.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 15
    • 0034640510 scopus 로고    scopus 로고
    • Protein kinase A associates with cystic fibrosis transmembrane conductance regulator via an interaction with ezrin
    • Sun, F., M. J. Hug, N. A. Bradbury, and R. A. Frizzell. 2000. Protein kinase A associates with cystic fibrosis transmembrane conductance regulator via an interaction with ezrin. J. Biol. Chem. 275: 14360-14366.
    • (2000) J. Biol. Chem , vol.275 , pp. 14360-14366
    • Sun, F.1    Hug, M.J.2    Bradbury, N.A.3    Frizzell, R.A.4
  • 16
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation
    • Brdicka, T., D. Pavlistova, A. Leo, E. Bruyns, V. Korinek, P. Angelisova, J. Scherer, A. Shevchenko, I. Hilgert, J. Cerny, et al. 2000. Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J. Exp. Med. 191: 1591-1604.
    • (2000) J. Exp. Med , vol.191 , pp. 1591-1604
    • Brdicka, T.1    Pavlistova, D.2    Leo, A.3    Bruyns, E.4    Korinek, V.5    Angelisova, P.6    Scherer, J.7    Shevchenko, A.8    Hilgert, I.9    Cerny, J.10
  • 18
    • 0032947605 scopus 로고    scopus 로고
    • Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin
    • Gronholm, M., M. Sainio, F. Zhao, L. Heiska, A. Vaheri, and O. Carpen. 1999. Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin. J. Cell Sci. 112: 895-904.
    • (1999) J. Cell Sci , vol.112 , pp. 895-904
    • Gronholm, M.1    Sainio, M.2    Zhao, F.3    Heiska, L.4    Vaheri, A.5    Carpen, O.6
  • 19
    • 0037089135 scopus 로고    scopus 로고
    • Positional effects of short interfering RNAs targeting the human coagulation trigger tissue factor
    • Holen, T., M. Amarzguioui, M. T. Wiiger, E. Babaie, and H. Prydz. 2002. Positional effects of short interfering RNAs targeting the human coagulation trigger tissue factor. Nucleic Acids Res. 30: 1757-1766.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1757-1766
    • Holen, T.1    Amarzguioui, M.2    Wiiger, M.T.3    Babaie, E.4    Prydz, H.5
  • 20
    • 0031748984 scopus 로고    scopus 로고
    • Protein kinase A type I antagonist restores immune responses of T cells from HIV-infected patients
    • Aandahl, E. M., P. Aukrust, B. S. Skalhegg, F. Muller, S. S. Froland, V. Hansson, and K. Tasken. 1998. Protein kinase A type I antagonist restores immune responses of T cells from HIV-infected patients. FASEB J. 12: 855-862.
    • (1998) FASEB J , vol.12 , pp. 855-862
    • Aandahl, E.M.1    Aukrust, P.2    Skalhegg, B.S.3    Muller, F.4    Froland, S.S.5    Hansson, V.6    Tasken, K.7
  • 22
    • 0027378347 scopus 로고
    • Reciprocal regulation of mRNA and protein for subunits of cAMP-dependent protein kinase (RIα and Cα) by cAMP in a neoplastic B cell line (Reh)
    • Tasken, K., K. B. Andersson, B. S. Skalhegg, K. A. Tasken, V. Hansson, T. Jahnsen, and H. K. Blomhoff. 1993. Reciprocal regulation of mRNA and protein for subunits of cAMP-dependent protein kinase (RIα and Cα) by cAMP in a neoplastic B cell line (Reh). J. Biol. Chem. 268: 23483-23489.
    • (1993) J. Biol. Chem , vol.268 , pp. 23483-23489
    • Tasken, K.1    Andersson, K.B.2    Skalhegg, B.S.3    Tasken, K.A.4    Hansson, V.5    Jahnsen, T.6    Blomhoff, H.K.7
  • 23
    • 0026348474 scopus 로고
    • Interaction of the regulatory subunit (Rii) of cAMP-dependent protein-kinase with Rii-anchoring proteins occurs through an amphipathic helix binding motif
    • Carr, D. W., R. E. Stofkohahn, I. D. C. Fraser, S. M. Bishop, T. S. Acott, R. G. Brennan, and J. D. Scott. 1991. Interaction of the regulatory subunit (Rii) of cAMP-dependent protein-kinase with Rii-anchoring proteins occurs through an amphipathic helix binding motif. J. Biol. Chem. 266: 14188-14192.
    • (1991) J. Biol. Chem , vol.266 , pp. 14188-14192
    • Carr, D.W.1    Stofkohahn, R.E.2    Fraser, I.D.C.3    Bishop, S.M.4    Acott, T.S.5    Brennan, R.G.6    Scott, J.D.7
  • 24
    • 0345435932 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450
    • Witczak, O., B. S. Skalhegg, G. Keryer, M. Bornens, K. Tasken, T. Jahnsen, and S. Orstavik. 1999. Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. EMBO J. 18: 1858-1868.
    • (1999) EMBO J , vol.18 , pp. 1858-1868
    • Witczak, O.1    Skalhegg, B.S.2    Keryer, G.3    Bornens, M.4    Tasken, K.5    Jahnsen, T.6    Orstavik, S.7
  • 25
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits
    • Huang, L. J. S., K. Durick, J. A. Weiner, J. Chun, and S. S. Taylor. 1997. Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits. J. Biol. Chem. 272: 8057-8064.
    • (1997) J. Biol. Chem , vol.272 , pp. 8057-8064
    • Huang, L.J.S.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5
  • 26
    • 0030881687 scopus 로고    scopus 로고
    • D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
    • Huang, L. J. S., K. Durick, J. A. Weiner, J. Chun, and S. S. Taylor. 1997. D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain. Proc. Natl. Acad. Sci. USA 94: 11184-11189.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11184-11189
    • Huang, L.J.S.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5
  • 27
    • 0037470628 scopus 로고    scopus 로고
    • A kinase anchoring protein (AKAP) interaction and dimerization of the RI and RI regulatory subunits of protein kinase A in vivo by the yeast two hybrid system
    • Carlson, C. R., A. Ruppelt, and K. Tasken. 2003. A kinase anchoring protein (AKAP) interaction and dimerization of the RI and RI regulatory subunits of protein kinase A in vivo by the yeast two hybrid system. J. Mol. Biol. 327: 609-618.
    • (2003) J. Mol. Biol , vol.327 , pp. 609-618
    • Carlson, C.R.1    Ruppelt, A.2    Tasken, K.3
  • 28
    • 0035207765 scopus 로고    scopus 로고
    • Identification, localization, steroidogenesis of PAP7: A peripheral-type benzodiazepine receptor- and PKA (RIα)-associated protein
    • Li, H., B. Degenhardt, D. Tobin, Z. X. Yao, K. Tasken, and V. Papadopoulos. 2001. Identification, localization, steroidogenesis of PAP7: a peripheral-type benzodiazepine receptor- and PKA (RIα)-associated protein. Mol. Endocrinol. 15: 2211-2228.
    • (2001) Mol. Endocrinol , vol.15 , pp. 2211-2228
    • Li, H.1    Degenhardt, B.2    Tobin, D.3    Yao, Z.X.4    Tasken, K.5    Papadopoulos, V.6
  • 29
    • 0037083640 scopus 로고    scopus 로고
    • Identification and characterization of myeloid translocation gene 16b as a novel A kinase anchoring protein in T lymphocytes
    • Schillace, R. V., S. F. Andrews, G. A. Liberty, M. P. Davey, and D. W. Carr. 2002. Identification and characterization of myeloid translocation gene 16b as a novel A kinase anchoring protein in T lymphocytes. J. Immunol. 168: 1590-1599.
    • (2002) J. Immunol , vol.168 , pp. 1590-1599
    • Schillace, R.V.1    Andrews, S.F.2    Liberty, G.A.3    Davey, M.P.4    Carr, D.W.5
  • 30
    • 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
  • 32
    • 0034724570 scopus 로고    scopus 로고
    • Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding
    • Herberg, F. W., A. Maleszka, T. Eide, L. Vossebein, and K. Tasken. 2000. Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding. J. Mol. Biol. 298: 329-339.
    • (2000) J. Mol. Biol , vol.298 , pp. 329-339
    • Herberg, F.W.1    Maleszka, A.2    Eide, T.3    Vossebein, L.4    Tasken, K.5
  • 35
    • 0038719674 scopus 로고    scopus 로고
    • Combined spatial and enzymatic regulation of Csk by cAMP and protein kinase A inhibits T cell receptor signaling
    • Vang, T., H. Abrahamsen, S. Myklebust, V. Horejsi, and K. Tasken. 2003. Combined spatial and enzymatic regulation of Csk by cAMP and protein kinase A inhibits T cell receptor signaling. J. Biol. Chem. 278: 17597-17600.
    • (2003) J. Biol. Chem , vol.278 , pp. 17597-17600
    • Vang, T.1    Abrahamsen, H.2    Myklebust, S.3    Horejsi, V.4    Tasken, K.5
  • 36
    • 0035955452 scopus 로고    scopus 로고
    • Interaction between two adapter proteins, PAG and EBP50: A possible link between membrane rafts and actin cytoskeleton
    • Brdickova, N., T. Brdicka, L. Andera, J. Spicka, P. Angelisova, S. L. Milgram, and V. Horejsi. 2001. Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton. FEBS Lett. 507: 133-136.
    • (2001) FEBS Lett , vol.507 , pp. 133-136
    • Brdickova, N.1    Brdicka, T.2    Andera, L.3    Spicka, J.4    Angelisova, P.5    Milgram, S.L.6    Horejsi, V.7
  • 37
    • 0031434473 scopus 로고    scopus 로고
    • Anchoring of protein kinase A facilitates hormone-mediated insulin secretion
    • Lester, L. B., L. K. Langeberg, and J. D. Scott. 1997. Anchoring of protein kinase A facilitates hormone-mediated insulin secretion. Proc. Natl. Acad. Sci. USA 94: 14942-14947.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14942-14947
    • Lester, L.B.1    Langeberg, L.K.2    Scott, J.D.3
  • 38
    • 0032545434 scopus 로고    scopus 로고
    • Identification of tethering domains for protein kinase A type Iα regulatory subunits on sperm fibrous sheath protein FSC1
    • Miki, K., and E. M. Eddy. 1998. Identification of tethering domains for protein kinase A type Iα regulatory subunits on sperm fibrous sheath protein FSC1. J. Biol. Chem. 273: 34384-34390.
    • (1998) J. Biol. Chem , vol.273 , pp. 34384-34390
    • Miki, K.1    Eddy, E.M.2
  • 39
    • 0034235485 scopus 로고    scopus 로고
    • Localization of a novel human A-kinase-anchoring protein, hAKAP220, during spermatogenesis
    • Reinton, N., P. Collas, T. B. Haugen, B. S. Skalhegg, V. Hansson, T. Jahnsen, and K. Tasken. 2000. Localization of a novel human A-kinase-anchoring protein, hAKAP220, during spermatogenesis. Dev. Biol. 223: 194-204.
    • (2000) Dev. Biol , vol.223 , pp. 194-204
    • Reinton, N.1    Collas, P.2    Haugen, T.B.3    Skalhegg, B.S.4    Hansson, V.5    Jahnsen, T.6    Tasken, K.7
  • 40
    • 0028810676 scopus 로고
    • Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells
    • Lin, R. Y., S. B. Moss, and C. S. Rubin. 1995. Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells. J. Biol. Chem. 270: 27804.
    • (1995) J. Biol. Chem , vol.270 , pp. 27804
    • Lin, R.Y.1    Moss, S.B.2    Rubin, C.S.3
  • 41
    • 0030570773 scopus 로고    scopus 로고
    • Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain
    • Trendelenburg, G., M. Hummel, E. O. Riecken, and C. Hanski. 1996. Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain. Biochem. Biophys. Res. Commun. 225: 313-319.
    • (1996) Biochem. Biophys. Res. Commun , vol.225 , pp. 313-319
    • Trendelenburg, G.1    Hummel, M.2    Riecken, E.O.3    Hanski, C.4
  • 43
    • 33746362123 scopus 로고    scopus 로고
    • Delineation of type I protein kinase A-selective signaling events using an RI anchoring disruptor
    • Carlson, C. R., B. Lygren, T. Berge, N. Hoshi, W. Wong, K. Tasken, and J. D. Scott. 2006. Delineation of type I protein kinase A-selective signaling events using an RI anchoring disruptor. J. Biol. Chem. 281: 21535-21545.
    • (2006) J. Biol. Chem , vol.281 , pp. 21535-21545
    • Carlson, C.R.1    Lygren, B.2    Berge, T.3    Hoshi, N.4    Wong, W.5    Tasken, K.6    Scott, J.D.7
  • 44
    • 0034631843 scopus 로고    scopus 로고
    • Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane
    • Gautreau, A., D. Louvard, and M. Arpin. 2000. Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane. J. Cell Biol. 150: 193-203.
    • (2000) J. Cell Biol , vol.150 , pp. 193-203
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 45
    • 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, S. Tsukita, 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    Tsukita, S.8
  • 46
    • 0029569120 scopus 로고
    • Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets
    • Nakamura, F., M. R. Amieva, and H. Furthmayr. 1995. Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. J. Biol. Chem. 270: 31377-31385.
    • (1995) J. Biol. Chem , vol.270 , pp. 31377-31385
    • Nakamura, F.1    Amieva, M.R.2    Furthmayr, H.3
  • 47
    • 0035831501 scopus 로고    scopus 로고
    • Hierarchy of merlin and ezrin N- and C-terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP
    • Nguyen, R., D. Reczek, and A. Bretscher. 2001. Hierarchy of merlin and ezrin N- and C-terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP. J. Biol. Chem. 276: 7621-7629.
    • (2001) J. Biol. Chem , vol.276 , pp. 7621-7629
    • Nguyen, R.1    Reczek, D.2    Bretscher, A.3
  • 48
    • 0034095211 scopus 로고    scopus 로고
    • Ezrin links syndecan-2 to the cytoskeleton
    • Granes, F., J. M. Urena, N. Rocamora, and S. Vilaro. 2000. Ezrin links syndecan-2 to the cytoskeleton. J. Cell Sci. 113: 1267-1276.
    • (2000) J. Cell Sci , vol.113 , pp. 1267-1276
    • Granes, F.1    Urena, J.M.2    Rocamora, N.3    Vilaro, S.4
  • 49
    • 0037902559 scopus 로고    scopus 로고
    • Protein kinase C-θ (PKCθ): It's all about location, location, location
    • Altman, A., and M. Villalba. 2003. Protein kinase C-θ (PKCθ): it's all about location, location, location. Immunol. Rev. 192: 53-63.
    • (2003) Immunol. Rev , vol.192 , pp. 53-63
    • Altman, A.1    Villalba, M.2
  • 50
    • 0033625869 scopus 로고    scopus 로고
    • Protein kinase Cθ: A new essential superstar on the T-cell stage
    • Altman, A., N. Isakov, and G. Baier. 2000. Protein kinase Cθ: a new essential superstar on the T-cell stage. Immunol. Today 21: 567-573.
    • (2000) Immunol. Today , vol.21 , pp. 567-573
    • Altman, A.1    Isakov, N.2    Baier, G.3
  • 51
    • 0037392883 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation through kinases and phosphatases
    • Mustelin, T., and K. Tasken. 2003. Positive and negative regulation of T-cell activation through kinases and phosphatases. Biochem. J. 371: 15-27.
    • (2003) Biochem. J , vol.371 , pp. 15-27
    • Mustelin, T.1    Tasken, K.2
  • 52
    • 0344826472 scopus 로고    scopus 로고
    • Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization
    • Brown, M. J., R. Nijhara, J. A. Hallam, M. Gignac, K. M. Yamada, S. L. Erlandsen, J. Delon, M. Kruhlak, and S. Shaw. 2003. Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization. Blood 102: 3890-3899.
    • (2003) Blood , vol.102 , pp. 3890-3899
    • Brown, M.J.1    Nijhara, R.2    Hallam, J.A.3    Gignac, M.4    Yamada, K.M.5    Erlandsen, S.L.6    Delon, J.7    Kruhlak, M.8    Shaw, S.9
  • 55
    • 27944447718 scopus 로고    scopus 로고
    • The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function
    • Dobenecker, M. W., C. Schmedt, M. Okada, and A. Tarakhovsky. 2005. The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function. Mol. Cell. Biol. 25: 10533-10542.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 10533-10542
    • Dobenecker, M.W.1    Schmedt, C.2    Okada, M.3    Tarakhovsky, A.4
  • 56
    • 25444448196 scopus 로고    scopus 로고
    • Cbp deficiency alters Csk localization in lipid rafts but does not affect T-cell development
    • Xu, S., J. Huo, J. E. Tan, and K. P. Lam. 2005. Cbp deficiency alters Csk localization in lipid rafts but does not affect T-cell development. Mol. Cell. Biol. 25: 8486-8495.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8486-8495
    • Xu, S.1    Huo, J.2    Tan, J.E.3    Lam, K.P.4
  • 57
    • 0029120438 scopus 로고
    • Negative regulation of T-cell adhesion and activation by Cd43
    • Manjunath, N., M. Correa, M. Ardman, and B. Ardman. 1995. Negative regulation of T-cell adhesion and activation by Cd43. Nature 377: 535-538.
    • (1995) Nature , vol.377 , pp. 535-538
    • Manjunath, N.1    Correa, M.2    Ardman, M.3    Ardman, B.4
  • 58
    • 0033120554 scopus 로고    scopus 로고
    • Structural requirements for CD43 function
    • Walker, J., and J. M. Green. 1999. Structural requirements for CD43 function. J. Immunol. 162: 4109-4114.
    • (1999) J. Immunol , vol.162 , pp. 4109-4114
    • Walker, J.1    Green, J.M.2
  • 60
    • 0032534304 scopus 로고    scopus 로고
    • Cutting edge: TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site
    • Sperling, A. I., J. R. Sedy, N. Manjunath, A. Kupfer, B. Ardman, and J. K. Burkhardt. 1998. Cutting edge: TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site. J. Immunol. 161: 6459-6462.
    • (1998) J. Immunol , vol.161 , pp. 6459-6462
    • Sperling, A.I.1    Sedy, J.R.2    Manjunath, N.3    Kupfer, A.4    Ardman, B.5    Burkhardt, J.K.6
  • 61
    • 2442472174 scopus 로고    scopus 로고
    • CD43 regulation of T cell activation is not through steric inhibition of T cell-APC interactions but through an intracellular mechanism
    • Tong, J. K., E. J. Allenspach, S. M. Takahashi, P. D. Mody, C. Park, J. K. Burkhardt, and A. I. Sperling. 2004. CD43 regulation of T cell activation is not through steric inhibition of T cell-APC interactions but through an intracellular mechanism. J. Exp. Med. 199: 1277-1283.
    • (2004) J. Exp. Med , vol.199 , pp. 1277-1283
    • Tong, J.K.1    Allenspach, E.J.2    Takahashi, S.M.3    Mody, P.D.4    Park, C.5    Burkhardt, J.K.6    Sperling, A.I.7
  • 62
    • 0037100399 scopus 로고    scopus 로고
    • Inhibition of antigen-specific T cell proliferation and cytokine production by protein kinase A type I
    • Aandahl, E. M., W. J. Moretto, P. A. Haslett, T. Vang, T. Bryn, K. Tasken, and D. F. Nixon. 2002. Inhibition of antigen-specific T cell proliferation and cytokine production by protein kinase A type I. J. Immunol. 169: 802-808.
    • (2002) J. Immunol , vol.169 , pp. 802-808
    • Aandahl, E.M.1    Moretto, W.J.2    Haslett, P.A.3    Vang, T.4    Bryn, T.5    Tasken, K.6    Nixon, D.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.