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Volumn 163, Issue 12, 1999, Pages 6589-6597

Distinct subcellular localization and substrate specificity of extracellular signal-regulated kinase in B cells upon stimulation with IgM and CD40

Author keywords

[No Author keywords available]

Indexed keywords

CD40 ANTIGEN; IMMUNOGLOBULIN M; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 0032756130     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (84)
  • 2
    • 0030890949 scopus 로고    scopus 로고
    • Initiation and processing of signals from the B cell antigen receptor
    • Reth, M., and J. Wienands. 1997. Initiation and processing of signals from the B cell antigen receptor. Annu. Rev. Immunol. 15:453.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 453
    • Reth, M.1    Wienands, J.2
  • 3
    • 0027943499 scopus 로고
    • A novel RING finger protein interacts with the cytoplasmic domain of CD40
    • Hu, H. M., K. O'Rourke, M. S. Bouguski, and V. M. Dixit. 1994. A novel RING finger protein interacts with the cytoplasmic domain of CD40. J. Biol. Chem. 269:30069.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30069
    • Hu, H.M.1    O'Rourke, K.2    Bouguski, M.S.3    Dixit, V.M.4
  • 4
    • 0028809176 scopus 로고
    • A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40
    • Sato, T., S. Irie, and J. C. Reed. 1995. A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40. FEBS Lett. 358:113.
    • (1995) FEBS Lett. , vol.358 , pp. 113
    • Sato, T.1    Irie, S.2    Reed, J.C.3
  • 6
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NFκB by TNF receptor 2 and CD40
    • Rothe, M., V. Sarma, V. M. Dixit, and D. V. Goeddel. 1995. TRAF2-mediated activation of NFκB by TNF receptor 2 and CD40. Science 269:1424.
    • (1995) Science , vol.269 , pp. 1424
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 8
    • 10544243364 scopus 로고    scopus 로고
    • Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor family protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region
    • Ishida, T., S. I. Mizushima, S. Azuma, N. Kobayashi, T. Tojo, K. Suzuki, S. Aizawa, T. Watanabe, G. Mosialos, E. Kief, T. Yamamoto, and J. Inoue. 1996. Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor family protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region. J. Biol. Chem. 271:28745.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28745
    • Ishida, T.1    Mizushima, S.I.2    Azuma, S.3    Kobayashi, N.4    Tojo, T.5    Suzuki, K.6    Aizawa, S.7    Watanabe, T.8    Mosialos, G.9    Kief, E.10    Yamamoto, T.11    Inoue, J.12
  • 9
    • 0028276378 scopus 로고
    • CD40 signaling pathway: Anti-CD40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine-phosphorylated proteins including protein tyrosine kinase Lyn, Fyn, and Syk and the appearance of a 28-kD tyrosine phosphorylated protein
    • Faris, M., F. Gaskin, J. T. Parsons, and S. M. Fu. 1994. CD40 signaling pathway: anti-CD40 monoclonal antibody induces rapid dephosphorylation and phosphorylation of tyrosine-phosphorylated proteins including protein tyrosine kinase Lyn, Fyn, and Syk and the appearance of a 28-kD tyrosine phosphorylated protein. J. Exp. Med. 179:1923.
    • (1994) J. Exp. Med. , vol.179 , pp. 1923
    • Faris, M.1    Gaskin, F.2    Parsons, J.T.3    Fu, S.M.4
  • 11
    • 0026012185 scopus 로고
    • Cross-linking of surface IgM activates NF-κB in B lymphocytes
    • Rosney, J. W., P. M. Dubois, and C. H. Sibley. 1991. Cross-linking of surface IgM activates NF-κB in B lymphocytes. Eur. J. Immunol. 21:2993.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 2993
    • Rosney, J.W.1    Dubois, P.M.2    Sibley, C.H.3
  • 12
    • 0028450096 scopus 로고
    • Induction of NF-AT in normal B lymphocytes by anti-immunoglobulin or CD40 ligand in conjunction with IL-4
    • Choi, M. S., R. D. Brines, M. J. Holman, and G. G. Klaus. 1994. Induction of NF-AT in normal B lymphocytes by anti-immunoglobulin or CD40 ligand in conjunction with IL-4. Immunity 1:179.
    • (1994) Immunity , vol.1 , pp. 179
    • Choi, M.S.1    Brines, R.D.2    Holman, M.J.3    Klaus, G.G.4
  • 14
    • 0028152658 scopus 로고
    • Cross-linking CD40 on B cells rapidly activates nuclear factor-κB
    • Berberich, I., G. L. Shu, and E. A. Clark. 1994. Cross-linking CD40 on B cells rapidly activates nuclear factor-κB. J. Immunol. 153:4357.
    • (1994) J. Immunol. , vol.153 , pp. 4357
    • Berberich, I.1    Shu, G.L.2    Clark, E.A.3
  • 15
    • 0028246272 scopus 로고
    • Cross-linking of surface IgM stimulates the Ras/Raf-1/ MEK/MAPK cascade in human B lymphocytes
    • Tordai, A., R. A. Franklin, H. Patel, A. M. Gardner, G. L. Johnson, and E. W. Gelfand. 1994. Cross-linking of surface IgM stimulates the Ras/Raf-1/ MEK/MAPK cascade in human B lymphocytes. J. Biol. Chem. 269:7538.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7538
    • Tordai, A.1    Franklin, R.A.2    Patel, H.3    Gardner, A.M.4    Johnson, G.L.5    Gelfand, E.W.6
  • 16
    • 0030069905 scopus 로고    scopus 로고
    • Cross-linking CD40 on B cells preferentially induces stress-activated protein kinases rather than mitogen-activated protein kinases
    • Berberich, I., G. Shu, F. Siebelt, J. R. Woodgett, J. M. Kyriakis, and E. A. Clark. 1996. Cross-linking CD40 on B cells preferentially induces stress-activated protein kinases rather than mitogen-activated protein kinases. EMBO J. 15:92.
    • (1996) EMBO J. , vol.15 , pp. 92
    • Berberich, I.1    Shu, G.2    Siebelt, F.3    Woodgett, J.R.4    Kyriakis, J.M.5    Clark, E.A.6
  • 17
    • 0030014424 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases via CD40 is distinct from that stimulated by surface IgM on B cells
    • Kashiwada, M., Y. Kaneko, H. Yagita, K. Okumura, and T. Takemori. 1996. Activation of mitogen-activated protein kinases via CD40 is distinct from that stimulated by surface IgM on B cells. Eur. J. Immunol. 26:1451.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1451
    • Kashiwada, M.1    Kaneko, Y.2    Yagita, H.3    Okumura, K.4    Takemori, T.5
  • 18
    • 0030586679 scopus 로고    scopus 로고
    • CD40 ligation results in protein kinase C-independent activation of ERK and JNK in resting murine splenic B cells
    • Li, Y. Y., M. Bacama, S. B. Waters, J. E. Pessin, G. A. Bishop, and G. A. Koretzky. 1996. CD40 ligation results in protein kinase C-independent activation of ERK and JNK in resting murine splenic B cells. J. Immunol. 157: 1440.
    • (1996) J. Immunol. , vol.157 , pp. 1440
    • Li, Y.Y.1    Bacama, M.2    Waters, S.B.3    Pessin, J.E.4    Bishop, G.A.5    Koretzky, G.A.6
  • 19
    • 0032032885 scopus 로고    scopus 로고
    • Differential coupling of membrane Ig and CD40 to the extracellularly regulated kinase signaling pathway
    • Purkerson, J. M., and D. C. Parker. 1998. Differential coupling of membrane Ig and CD40 to the extracellularly regulated kinase signaling pathway. J. Immunol. 160:2121.
    • (1998) J. Immunol. , vol.160 , pp. 2121
    • Purkerson, J.M.1    Parker, D.C.2
  • 20
    • 0031975588 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway
    • Kashiwada, M., Y. Shirakata, J. I. Inoue, H. Nakano, K. Okazaki, K. Okumura, T. Yamamoto, H. Nagaoka, and T. Takemori. 1998. Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway. J. Exp. Med. 187:237.
    • (1998) J. Exp. Med. , vol.187 , pp. 237
    • Kashiwada, M.1    Shirakata, Y.2    Inoue, J.I.3    Nakano, H.4    Okazaki, K.5    Okumura, K.6    Yamamoto, T.7    Nagaoka, H.8    Takemori, T.9
  • 21
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis, R. J. 1993. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268:14553.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14553
    • Davis, R.J.1
  • 22
    • 0028859281 scopus 로고
    • Selective requirement for MAP kinase activation in thymocyte differentiation
    • Alberola, I. J., K. A. Forbush, R. Seger, E. G. Krebs, and R. M. Perlmutter. 1995. Selective requirement for MAP kinase activation in thymocyte differentiation. Nature 373:620.
    • (1995) Nature , vol.373 , pp. 620
    • Alberola, I.J.1    Forbush, K.A.2    Seger, R.3    Krebs, E.G.4    Perlmutter, R.M.5
  • 24
    • 0030664126 scopus 로고    scopus 로고
    • Control of B cell development by Ras-mediated activation of Raf
    • Iritani, B. M., K. A. Forbush, M. A. Farrar, and R. M. Perlmutter. 1997. Control of B cell development by Ras-mediated activation of Raf. EMBO J. 16:7019.
    • (1997) EMBO J. , vol.16 , pp. 7019
    • Iritani, B.M.1    Forbush, K.A.2    Farrar, M.A.3    Perlmutter, R.M.4
  • 25
    • 0030972494 scopus 로고    scopus 로고
    • Interaction of MAP kinase with MAP kinase kinase: Its possible role in the control of nucleocytoplasmic transport of MAP kinase
    • Fukuda, M., Y. Gotoh, and E. Nishida. 1997. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J. 16:1901.
    • (1997) EMBO J. , vol.16 , pp. 1901
    • Fukuda, M.1    Gotoh, Y.2    Nishida, E.3
  • 27
    • 0027283659 scopus 로고
    • Growth factors induce nuclear translocation of MAP kinases (p42 mapk and p44 mapk) but not of their activator MAP kinase kinase (p45 mapkk) in fibroblasts
    • Lenormand, P., C. Sardet, G. Pages, G. L'Allemain, A. Brunet, and J. Pouyssegur. 1993. Growth factors induce nuclear translocation of MAP kinases (p42 mapk and p44 mapk) but not of their activator MAP kinase kinase (p45 mapkk) in fibroblasts. J. Cell Biol. 122:1079.
    • (1993) J. Cell Biol. , vol.122 , pp. 1079
    • Lenormand, P.1    Sardet, C.2    Pages, G.3    L'Allemain, G.4    Brunet, A.5    Pouyssegur, J.6
  • 28
    • 0027225936 scopus 로고
    • Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus
    • Gonzalez, F. A., A. Seth, D. L. Raden, D. S. Bowman, F. S. Fay, and R. J. Davis. 1993. Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus. J. Cell Biol. 122:1089.
    • (1993) J. Cell Biol. , vol.122 , pp. 1089
    • Gonzalez, F.A.1    Seth, A.2    Raden, D.L.3    Bowman, D.S.4    Fay, F.S.5    Davis, R.J.6
  • 31
    • 0025871767 scopus 로고
    • Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation: Characterization of the phosphorylation of c-myc and c-jun protein by an epidermal growth factor receptor threonine 669 protein kinase
    • Alvarez, C., I. C. Northwood, F. A. Gonzalez, D. A. Latour, A. Seth, C. Abate, T. Curran, and D. J. Davis. 1991. Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation: characterization of the phosphorylation of c-myc and c-jun protein by an epidermal growth factor receptor threonine 669 protein kinase. J. Biol. Chem. 266:15277.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15277
    • Alvarez, C.1    Northwood, I.C.2    Gonzalez, F.A.3    Latour, D.A.4    Seth, A.5    Abate, C.6    Curran, T.7    Davis, D.J.8
  • 32
    • 0026695645 scopus 로고
    • Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter
    • Gille, H., A. D. Sharrocks, and P. E. Shaw, 1992. Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter. Nature 358:414.
    • (1992) Nature , vol.358 , pp. 414
    • Gille, H.1    Sharrocks, A.D.2    Shaw, P.E.3
  • 33
    • 0027067934 scopus 로고
    • Inhibition of c-Jun DNA binding by mitogen-activated protein kinase
    • Chou, S.-Y., V. Baichwal, and J. E. Ferrell, Jr. 1992. Inhibition of c-Jun DNA binding by mitogen-activated protein kinase. Mol. Cell. Biol. 3:1117.
    • (1992) Mol. Cell. Biol. , vol.3 , pp. 1117
    • Chou, S.-Y.1    Baichwal, V.2    Ferrell J.E., Jr.3
  • 34
    • 0027297647 scopus 로고
    • The SRF accessory protein ELK-1 contains a growth factor-regulated transcriptional activation domain
    • Marais, R., J. Wynne, and R. Treisman, 1993. The SRF accessory protein ELK-1 contains a growth factor-regulated transcriptional activation domain. Cell 73:381.
    • (1993) Cell , vol.73 , pp. 381
    • Marais, R.1    Wynne, J.2    Treisman, R.3
  • 35
    • 0027475972 scopus 로고
    • Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1
    • Cheng, J.-T., M. H. Cobb, and Baer, R. 1993. Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1. Mol. Cell. Biol. 13:801.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 801
    • Cheng, J.-T.1    Cobb, M.H.2    Baer, R.3
  • 36
    • 0027499295 scopus 로고
    • Phosphorylation at threonine-235 by a ras-dependent mitogen-activated protein kinase cascade is essential for transcription factor NF-IL6
    • Nakajima, T., S. Kinoshita, T. Sasagawa, K. Sasaki, M. Naruto, T. Kishimoto, and T. Hirano. 1993. Phosphorylation at threonine-235 by a ras-dependent mitogen-activated protein kinase cascade is essential for transcription factor NF-IL6. Proc. Natl. Acad. Sci. USA 90:2207.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2207
    • Nakajima, T.1    Kinoshita, S.2    Sasagawa, T.3    Sasaki, K.4    Naruto, M.5    Kishimoto, T.6    Hirano, T.7
  • 37
    • 0028099773 scopus 로고
    • Enhanced phosphorylation of the C-terminal domain of RNA polmerase II upon serum stimulation of quiescent cells: Possible involvement of MAP kinase
    • Dubois, M. F., V. T. Nguyen, M. E. Dahmus, G. Pages, J. Pouyssegur, and O. Bensaude. 1994. Enhanced phosphorylation of the C-terminal domain of RNA polmerase II upon serum stimulation of quiescent cells: possible involvement of MAP kinase. EMBO J. 13:4787.
    • (1994) EMBO J. , vol.13 , pp. 4787
    • Dubois, M.F.1    Nguyen, V.T.2    Dahmus, M.E.3    Pages, G.4    Pouyssegur, J.5    Bensaude, O.6
  • 38
    • 0029133702 scopus 로고
    • Requirement for MAP kinase (ERK2) activity in interferon α-and interferon β-stimulated gene expression through STAT protein
    • David, M., E. Petricoin, III, C. Benjamin, R. Pine, M. J. Weber, and A. C Larnen. 1995. Requirement for MAP kinase (ERK2) activity in interferon α-and interferon β-stimulated gene expression through STAT protein. Science 269:1721.
    • (1995) Science , vol.269 , pp. 1721
    • David, M.1    Petricoin E. III2    Benjamin, C.3    Pine, R.4    Weber, M.J.5    Larnen, A.C.6
  • 39
    • 0025917268 scopus 로고
    • Isolation and characterization of two growth factor-stimulated protein kinases that phosphorylate the epidermal growth factor receptor at threonine 669
    • Northwood, I. C., F. A. Gonzalez, M. Wartmann, D. L. Raden, and R. J. Davis. 1991. Isolation and characterization of two growth factor-stimulated protein kinases that phosphorylate the epidermal growth factor receptor at threonine 669. J. Biol. Chem. 266:15266.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15266
    • Northwood, I.C.1    Gonzalez, F.A.2    Wartmann, M.3    Raden, D.L.4    Davis, R.J.5
  • 40
    • 0026088781 scopus 로고
    • Epidermal growth factor (EGF) receptor T669 peptide kinase from 3T3-L1 cells is an EGF-mimulated "MAP" kinase
    • Takishima, K., I. Griswold-Prenner, T. Ingebritsen, and M. R. Rosner. 1991. Epidermal growth factor (EGF) receptor T669 peptide kinase from 3T3-L1 cells is an EGF-Mimulated "MAP" kinase. Proc. Natl. Acad. Sci. USA 88:2520.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2520
    • Takishima, K.1    Griswold-Prenner, I.2    Ingebritsen, T.3    Rosner, M.R.4
  • 42
    • 0027513768 scopus 로고
    • Phosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase kinase and MAP kinase
    • Matsuda, S., Y. Gotoh, and E. Nishida. 1993. Phosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase kinase and MAP kinase. J. Biol. Chem. 268:3277.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3277
    • Matsuda, S.1    Gotoh, Y.2    Nishida, E.3
  • 43
    • 0029826107 scopus 로고    scopus 로고
    • CD40-mediated stimulation of B1 and B2 cells: Implication in autoantibody production in murine lupus
    • Kaneko, Y., S. Hirose, M. Abe, H. Yagita, K. Okumura, and T. Shirai. 1996. CD40-mediated stimulation of B1 and B2 cells: implication in autoantibody production in murine lupus. Eur. J. Immunol. 26:3061.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 3061
    • Kaneko, Y.1    Hirose, S.2    Abe, M.3    Yagita, H.4    Okumura, K.5    Shirai, T.6
  • 46
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of erk-and rsk-encoded protein kinases
    • Chen, R-.H., C. Sarnecki, and J. Blenis. 1992. Nuclear localization and regulation of erk-and rsk-encoded protein kinases. Mol. Cell. Biol. 12:915.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 915
    • Chen, R.-.H.1    Sarnecki, C.2    Blenis, J.3
  • 47
    • 0016775871 scopus 로고
    • Colchicine permeation is required for inhibition of concanavalin A capping in Chinese hamster ovary cells
    • Aubin, J. E., S. A. Carlsen, and V. Ling. 1975. Colchicine permeation is required for inhibition of concanavalin A capping in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 72:4516.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4516
    • Aubin, J.E.1    Carlsen, S.A.2    Ling, V.3
  • 48
    • 0020029505 scopus 로고
    • Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro
    • Yahara, I., F. Harada, S. Sekita, K. Yoshihira, and S. Natori. 1982. Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro. J. Cell Biol. 92:69.
    • (1982) J. Cell Biol. , vol.92 , pp. 69
    • Yahara, I.1    Harada, F.2    Sekita, S.3    Yoshihira, K.4    Natori, S.5
  • 49
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation
    • Yamaoka, S., G. Courtois, C. Bessia, S. T. Whiteside, R. Weil, F. Agou, H. E. Kirk, R. J. Kay, and A. Israel, 1998. Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation. Cell 93:1231.
    • (1998) Cell , vol.93 , pp. 1231
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6    Kirk, H.E.7    Kay, R.J.8    Israel, A.9
  • 50
    • 0032541657 scopus 로고    scopus 로고
    • 1KK-γ is an essential regulatory subunitt of the IκB kinase complex
    • Rothwarf, D. M., E. Zandi, G. Natoli, M. Karin. 1998. 1KK-γ is an essential regulatory subunitt of the IκB kinase complex. Nature 395:297.
    • (1998) Nature , vol.395 , pp. 297
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 51
    • 0025375345 scopus 로고
    • Functional domains and upstream activation properties of cloned human TATA binding protein
    • Peterson, M. G., N. Tanese, B. F. Pugh, and R. Tjian. 1990. Functional domains and upstream activation properties of cloned human TATA binding protein. Science 248:1625.
    • (1990) Science , vol.248 , pp. 1625
    • Peterson, M.G.1    Tanese, N.2    Pugh, B.F.3    Tjian, R.4
  • 52
  • 53
    • 0344737208 scopus 로고
    • A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that are each similar to distinct protein kinase
    • Jones, S. W., E. Erikson, J. Blenis, J. Maller, and R. L. Erikson. 1988. A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that are each similar to distinct protein kinase. Proc. Natl. Acad. Sci. USA 85:3377.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3377
    • Jones, S.W.1    Erikson, E.2    Blenis, J.3    Maller, J.4    Erikson, R.L.5
  • 54
    • 0025305456 scopus 로고
    • Identification of mitogen-responsive ribosomal protein S6 kinase pp90rsk, a homologue of Xenopus S6 kinase II. In chicken embryo fibroblasts
    • Sweet, L. J., D. A. Alcorta, S. W. Jones, E. Erikson, and R. L. Erikson. 1990. Identification of mitogen-responsive ribosomal protein S6 kinase pp90rsk, a homologue of Xenopus S6 kinase II. in chicken embryo fibroblasts. Mol. Cell. Biol. 10:2413.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2413
    • Sweet, L.J.1    Alcorta, D.A.2    Jones, S.W.3    Erikson, E.4    Erikson, R.L.5
  • 55
    • 0025924682 scopus 로고
    • Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro
    • Chung, J., R. H. Chen, and J. Blenis. 1991. Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro. Mol. Cell. Biol. 11:1868.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1868
    • Chung, J.1    Chen, R.H.2    Blenis, J.3
  • 56
    • 0027156503 scopus 로고
    • Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90-kDa ribosomal S6 kinase in PC12 cells: Distinct effects of the neurotropic factor, nerve growth factor, and the mitogen factor, epidermal growth factor
    • Nguyen, T. T., J.-C. Seimeca, C. Filloux, P. Peraldi, J. L. Carpentier, and E. Van Obberghen. 1993. Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90-kDa ribosomal S6 kinase in PC12 cells: distinct effects of the neurotropic factor, nerve growth factor, and the mitogen factor, epidermal growth factor. J. Biol. Chem. 268:9803.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9803
    • Nguyen, T.T.1    Seimeca, J.-C.2    Filloux, C.3    Peraldi, P.4    Carpentier, J.L.5    Van Obberghen, E.6
  • 57
    • 0027328572 scopus 로고
    • Regulation of an epitope-tagged recombinant Rsk-1 S6 kinase by phorbol ester and erk/MAP kinase
    • Grove, J. R., D. J. Price, P. Banerjee, A. Balasubramanyam, M. F. Ahmad, and J. Avruch. 1993. Regulation of an epitope-tagged recombinant Rsk-1 S6 kinase by phorbol ester and erk/MAP kinase. Biochemistry 32:7727.
    • (1993) Biochemistry , vol.32 , pp. 7727
    • Grove, J.R.1    Price, D.J.2    Banerjee, P.3    Balasubramanyam, A.4    Ahmad, M.F.5    Avruch, J.6
  • 58
    • 0027400484 scopus 로고
    • Identification of insulin-stimulated protein kinase-1 as the rabbit equivalent of rskmo-2: Identification of two threonines phosphorylated during activation by mitogen-activated protein kinase
    • Sutherland, C., D. G. Campbell, and P. Cohen, 1993 Identification of insulin-stimulated protein kinase-1 as the rabbit equivalent of rskmo-2: identification of two threonines phosphorylated during activation by mitogen-activated protein kinase. Eur. J. Biochem. 212:581.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 581
    • Sutherland, C.1    Campbell, D.G.2    Cohen, P.3
  • 59
    • 0028907351 scopus 로고
    • Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 s6 kinase and for insulin or serum stimulation of DNA synthesis
    • Sale, E. M., P. G. Atkinson, and G. J. Sale. 1995. Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 S6 kinase and for insulin or serum stimulation of DNA synthesis. EMBO J. 14:674.
    • (1995) EMBO J. , vol.14 , pp. 674
    • Sale, E.M.1    Atkinson, P.G.2    Sale, G.J.3
  • 60
    • 0029860520 scopus 로고    scopus 로고
    • Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases
    • Zhao, Y., C. Bjorbaek, and D. E. Moller. 1996. Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases. J. Biol. Chem. 271: 29773.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29773
    • Zhao, Y.1    Bjorbaek, C.2    Moller, D.E.3
  • 61
    • 0026517618 scopus 로고
    • Mitogen-activated-protein-kinase-catalyzed phosphorylation of microtubule-associated proteins, microtubule-associated protein 2 and microtubule-associated protein 4 induces an alteration in their function
    • Hoshi, M., K. Ohta, Y. Gotoh, A. Mori, H. Murofushi, H. Sakai, and E. Nishida. 1992. Mitogen-activated-protein-kinase-catalyzed phosphorylation of microtubule-associated proteins, microtubule-associated protein 2 and microtubule-associated protein 4 induces an alteration in their function. Eur. J. Biochem. 203:43.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 43
    • Hoshi, M.1    Ohta, K.2    Gotoh, Y.3    Mori, A.4    Murofushi, H.5    Sakai, H.6    Nishida, E.7
  • 62
    • 0029863927 scopus 로고    scopus 로고
    • Association of mitogen-activated protein kinases with microtubules in mouse macrophages
    • Ding, A., B. Chen, M. Fuortes, and E. Blum. 1996. Association of mitogen-activated protein kinases with microtubules in mouse macrophages. J. Exp. Med. 183:1899.
    • (1996) J. Exp. Med. , vol.183 , pp. 1899
    • Ding, A.1    Chen, B.2    Fuortes, M.3    Blum, E.4
  • 63
    • 0029943566 scopus 로고    scopus 로고
    • The pool of map kinase associated with microtubules is small but constitutively active
    • Morishima-Kawashima, M., and K. S. Kosik. 1996. The pool of map kinase associated with microtubules is small but constitutively active. Mol. Biol. Cell. 7:893.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 893
    • Morishima-Kawashima, M.1    Kosik, K.S.2
  • 64
    • 0010508313 scopus 로고
    • Addition of colchicine-tubulin complex to microtubule ends: The mechanism of substoichiometric colchicine poisoning
    • Margolis, R. L., and L. Wilson. 1977. Addition of colchicine-tubulin complex to microtubule ends: the mechanism of substoichiometric colchicine poisoning. Proc. Natl. Acad. Sci. USA 74:3466.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3466
    • Margolis, R.L.1    Wilson, L.2
  • 65
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179.
    • (1995) Cell , vol.80 , pp. 179
    • Marshall, C.J.1
  • 67
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Goerlich, D. 1998. Transport into and out of the cell nucleus. EMBO J. 17:2721.
    • (1998) EMBO J. , vol.17 , pp. 2721
    • Goerlich, D.1
  • 69
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao, A., C. Luo, and P. G. Hogan. 1997. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 15:707.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 70
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-κB
    • May, M. J., and S. Ghosh. 1998. Signal transduction through NF-κB. Immunol. Today 19:80.
    • (1998) Immunol. Today , vol.19 , pp. 80
    • May, M.J.1    Ghosh, S.2
  • 72
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the Ras-MAPK pathways to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing, J., D. D. Ginty, and M. E. Greenberg. 1996. Coupling of the Ras-MAPK pathways to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 273:959.
    • (1996) Science , vol.273 , pp. 959
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 74
    • 0030851775 scopus 로고    scopus 로고
    • rsk) phosphorylates the N-terminal regulatory domain of ikBα and stimulates its degradation in vitro
    • rsk) phosphorylates the N-terminal regulatory domain of IkBα and stimulates its degradation in vitro. J. Biol. Chem. 272:21281.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21281
    • Ghoda, L.1    Lin, X.2    Greene, W.C.3
  • 75
    • 0030767442 scopus 로고    scopus 로고
    • EGF induced SOS phosphorylation in PC12 cells involves P90 RSK-2
    • Douville, E., and J. Downward. 1997. EGF induced SOS phosphorylation in PC12 cells involves P90 RSK-2. Oncogene 15:373.
    • (1997) Oncogene , vol.15 , pp. 373
    • Douville, E.1    Downward, J.2
  • 76
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
    • Sontag, E., S. Fedorovo, C. Kamibayashi, D. Robbins, M. Cobb, and M. Mumby. 1993. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell 75:887.
    • (1993) Cell , vol.75 , pp. 887
    • Sontag, E.1    Fedorovo, S.2    Kamibayashi, C.3    Robbins, D.4    Cobb, M.5    Mumby, M.6
  • 77
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia, Z., M. Dickens, J. Raingeaud, R. J. Davis, and M. E. Greenberg. 1995. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270: 1326.
    • (1995) Science , vol.270 , pp. 1326
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 79
    • 0031000626 scopus 로고    scopus 로고
    • Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase
    • Wahlen, A. M., S. C. Galasinski, P. S. Shapiro, T. S. Nahreini, and N. G. Ahn. 1997. Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase. Mol. Cell. Biol. 17:1947.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1947
    • Wahlen, A.M.1    Galasinski, S.C.2    Shapiro, P.S.3    Nahreini, T.S.4    Ahn, N.G.5
  • 80
    • 0030707866 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte antigen 4 (CTLA-4) interferes with extracellular signal-regulated kinase (ERK) and Jun NH2-terminal kinase (JNK) activation, but does not affect phosphorylation of T cell receptor ζ and ZAP70
    • Calvo, C. R., D. Amsen, and A. M. Kruisbeek. 1997. Cytotoxic T lymphocyte antigen 4 (CTLA-4) interferes with extracellular signal-regulated kinase (ERK) and Jun NH2-terminal kinase (JNK) activation, but does not affect phosphorylation of T cell receptor ζ and ZAP70. J. Exp. Med. 186:1645.
    • (1997) J. Exp. Med. , vol.186 , pp. 1645
    • Calvo, C.R.1    Amsen, D.2    Kruisbeek, A.M.3
  • 82
    • 0028862078 scopus 로고
    • Role of B cell receptor Ig α and β subunits in MHC class II-restricted antigen presentation
    • Bonnerot, C., D. Lankar, D. Hanau, D. Spehner, J. Davoust, J. Salamero, and W. H. Fridman. 1995. Role of B cell receptor Ig α and β subunits in MHC class II-restricted antigen presentation. Immunity 3:335.
    • (1995) Immunity , vol.3 , pp. 335
    • Bonnerot, C.1    Lankar, D.2    Hanau, D.3    Spehner, D.4    Davoust, J.5    Salamero, J.6    Fridman, W.H.7
  • 84
    • 0032100715 scopus 로고    scopus 로고
    • Arrest of B lymphocyte terminal differentiation by CD40 signaling: Mechanism for lack of antibody-secreting cells in germinal center
    • Randall, T. D., A. W. Heath, L. S.-Argumedo, M. C. Howard, I. L. Weissman, and F. E. Lund. 1998. Arrest of B lymphocyte terminal differentiation by CD40 signaling: mechanism for lack of antibody-secreting cells in germinal center. Immunity 8:733.
    • (1998) Immunity , vol.8 , pp. 733
    • Randall, T.D.1    Heath, A.W.2    Argumedo, L.S.3    Howard, M.C.4    Weissman, I.L.5    Lund, F.E.6


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