메뉴 건너뛰기




Volumn 8, Issue 11, 2007, Pages 1227-1235

The MAPK-activated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 CHLORO 4 IODOANILINO) N CYCLOPROPYLMETHOXY 3,4 DIFLUOROBENZAMIDE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; DORAMAPIMOD; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE ACTIVATED KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE ACTIVATED KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; P90 RIBOSOMAL S6 KINASE; PROTEIN TYROSINE KINASE; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG;

EID: 35548930283     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni1517     Document Type: Article
Times cited : (112)

References (58)
  • 2
    • 33745712871 scopus 로고    scopus 로고
    • Reis e Sousa, C. Dendritic cells in a mature age. Nat. Rev. Immunol. 6, 476-483 (2006).
    • Reis e Sousa, C. Dendritic cells in a mature age. Nat. Rev. Immunol. 6, 476-483 (2006).
  • 3
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta, E.S. & Mellman, I. Cell biology of antigen processing in vitro and in vivo. Annu. Rev. Immunol. 23, 975-1028 (2005).
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 4
    • 0035957320 scopus 로고    scopus 로고
    • Mobilization of MHC class I molecules from late endosomes to the cell surface following activation of CD34-derived human Langerhans cells
    • MacAry, P.A. et al. Mobilization of MHC class I molecules from late endosomes to the cell surface following activation of CD34-derived human Langerhans cells. Proc. Natl. Acad. Sci. USA 98, 3982-3987 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3982-3987
    • MacAry, P.A.1
  • 5
    • 0037194733 scopus 로고    scopus 로고
    • Dendritic cell maturation triggers retrograde MHC class II transport from lysosomes to the plasma membrane
    • Chow, A., Toomre, D., Garrett, W. & Mellman, I. Dendritic cell maturation triggers retrograde MHC class II transport from lysosomes to the plasma membrane. Nature 418, 988-994 (2002).
    • (2002) Nature , vol.418 , pp. 988-994
    • Chow, A.1    Toomre, D.2    Garrett, W.3    Mellman, I.4
  • 6
    • 0035494424 scopus 로고    scopus 로고
    • Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells
    • Kleijmeer, M. et al. Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells. J. Cell Biol. 155, 53-63 (2001).
    • (2001) J. Cell Biol , vol.155 , pp. 53-63
    • Kleijmeer, M.1
  • 7
    • 33750593611 scopus 로고    scopus 로고
    • Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination
    • Shin, J.S. et al. Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination. Nature 444, 115-118 (2006).
    • (2006) Nature , vol.444 , pp. 115-118
    • Shin, J.S.1
  • 8
    • 33845397207 scopus 로고    scopus 로고
    • Dendritic cells regulate exposure of MHC class II at their plasma membrane by oligoubiquitination
    • van Niel, G. et al. Dendritic cells regulate exposure of MHC class II at their plasma membrane by oligoubiquitination. Immunity 25 885-894 (2006).
    • (2006) Immunity , vol.25 , pp. 885-894
    • van Niel, G.1
  • 9
    • 2342525996 scopus 로고    scopus 로고
    • Regulation of phagosome maturation by signals from toll-like receptors
    • Blander, J.M. & Medzhitov, R. Regulation of phagosome maturation by signals from toll-like receptors. Science 304, 1014-1018 (2004).
    • (2004) Science , vol.304 , pp. 1014-1018
    • Blander, J.M.1    Medzhitov, R.2
  • 10
    • 4143086928 scopus 로고    scopus 로고
    • Enhanced dendritic cell antigen capture via Toll-like receptor-induced actin remodeling
    • West, M.A. et al. Enhanced dendritic cell antigen capture via Toll-like receptor-induced actin remodeling. Science 305, 1153-1157 (2004).
    • (2004) Science , vol.305 , pp. 1153-1157
    • West, M.A.1
  • 11
    • 0037046536 scopus 로고    scopus 로고
    • Transient aggregation of ubiquitinated proteins during dendritic cell maturation
    • Lelouard, H. et al. Transient aggregation of ubiquitinated proteins during dendritic cell maturation. Nature 417, 177-182 (2002).
    • (2002) Nature , vol.417 , pp. 177-182
    • Lelouard, H.1
  • 12
    • 30044442866 scopus 로고    scopus 로고
    • How Toll-like receptors signal: What we know and what we don't know
    • O'Neill, L.A. How Toll-like receptors signal: What we know and what we don't know. Curr. Opin. Immunol. 18, 3-9 (2006).
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 3-9
    • O'Neill, L.A.1
  • 13
    • 33748320817 scopus 로고    scopus 로고
    • RSK and MSK in MAP kinase signalling
    • Hauge, C. & Frodin, M. RSK and MSK in MAP kinase signalling. J. Cell Sci. 119, 3021-3023 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 3021-3023
    • Hauge, C.1    Frodin, M.2
  • 14
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases-MKs-two's company, three's a crowd
    • Gaestel, M. MAPKAP kinases-MKs-two's company, three's a crowd. Nat. Rev. Mol. Cell Biol. 7, 120-130 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 120-130
    • Gaestel, M.1
  • 15
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • Roux, P.P. & Blenis, J. ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 68, 320-344 (2004).
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 16
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak, M., Clifton, A.D., Lucocq, L.M. & Alessi, D.R. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 17 4426-4441 (1998).
    • (1998) EMBO J , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 17
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz, A.J., Flynn, A., Proud, C.G. & Cooper, J.A. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16, 1909-1920 (1997).
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 18
    • 0242612949 scopus 로고    scopus 로고
    • A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1
    • Frodin, M., Jensen, C.J., Merienne, K. & Gammeltoft, S. A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1. EMBO J. 19, 2924-2934 (2000).
    • (2000) EMBO J , vol.19 , pp. 2924-2934
    • Frodin, M.1    Jensen, C.J.2    Merienne, K.3    Gammeltoft, S.4
  • 19
    • 0038112035 scopus 로고    scopus 로고
    • Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity
    • Roux, P.P., Richards, S.A. & Blenis, J. Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity. Mol. Cell Biol. 23, 4796-4804 (2003).
    • (2003) Mol. Cell Biol , vol.23 , pp. 4796-4804
    • Roux, P.P.1    Richards, S.A.2    Blenis, J.3
  • 20
    • 17144370207 scopus 로고    scopus 로고
    • Functional characterization of human RSK4, a new 90-kDa ribosomal S6 kinase, reveals constitutive activation in most cell types
    • Dummler, B.A. et al. Functional characterization of human RSK4, a new 90-kDa ribosomal S6 kinase, reveals constitutive activation in most cell types. J. Biol. Chem. 280, 13304-13314 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 13304-13314
    • Dummler, B.A.1
  • 22
    • 0030063435 scopus 로고    scopus 로고
    • Evidence for two catalytically active kinase domains in pp90rsk
    • Fisher, T.L. & Blenis, J. Evidence for two catalytically active kinase domains in pp90rsk. Mol. Cell. Biol. 16, 1212-1219 (1996).
    • (1996) Mol. Cell. Biol , vol.16 , pp. 1212-1219
    • Fisher, T.L.1    Blenis, J.2
  • 23
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • Frodin, M. et al. A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation. EMBO J. 21, 5396-5407 (2002).
    • (2002) EMBO J , vol.21 , pp. 5396-5407
    • Frodin, M.1
  • 24
    • 0037011121 scopus 로고    scopus 로고
    • Inhibition of SAPK2a/p38 prevents hnRNP AO phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs
    • Rousseau, S. et al. Inhibition of SAPK2a/p38 prevents hnRNP AO phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs. EMBO J. 21, 6505-6514 (2002).
    • (2002) EMBO J , vol.21 , pp. 6505-6514
    • Rousseau, S.1
  • 25
    • 0036479125 scopus 로고    scopus 로고
    • MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels
    • Neininger A. et al. MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels. J. Biol. Chem. 277, 3065-3068 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 3065-3068
    • Neininger, A.1
  • 26
    • 0033145354 scopus 로고    scopus 로고
    • MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis
    • Kotlyarov, A. et al. MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis. Nat. Cell Biol. 1, 94-97 (1999).
    • (1999) Nat. Cell Biol , vol.1 , pp. 94-97
    • Kotlyarov, A.1
  • 27
    • 0027482463 scopus 로고
    • Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27
    • Lavoie, J.N., Hickey, E., Weber, L.A. & Landry, J. Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. Biol. Chem. 268, 24210-24214 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 24210-24214
    • Lavoie, J.N.1    Hickey, E.2    Weber, L.A.3    Landry, J.4
  • 28
    • 0038182524 scopus 로고    scopus 로고
    • MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14
    • Soloaga, A. et al. MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14. EMBO J. 22, 2788-2797 (2003).
    • (2003) EMBO J , vol.22 , pp. 2788-2797
    • Soloaga, A.1
  • 29
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • Thomson, S. et al. The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. EMBO J. 18, 4779-4793 (1999).
    • (1999) EMBO J , vol.18 , pp. 4779-4793
    • Thomson, S.1
  • 30
    • 3242719457 scopus 로고    scopus 로고
    • Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development
    • Ueda, T., Watanabe-Fukunaga, R., Fukuyama, H., Nagata, S. & Fukunaga, R. Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development. Mol. Cell. Biol. 24, 6539-6549 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6539-6549
    • Ueda, T.1    Watanabe-Fukunaga, R.2    Fukuyama, H.3    Nagata, S.4    Fukunaga, R.5
  • 31
    • 21244476768 scopus 로고    scopus 로고
    • BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo
    • Kuma, Y. et al. BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo. J. Biol. Chem. 280, 19472-19479 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 19472-19479
    • Kuma, Y.1
  • 32
    • 33845807361 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK
    • Ronkina, N. et al. The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK. Mol Cell. Biol. 27, 170-181 (2007).
    • (2007) Mol Cell. Biol , vol.27 , pp. 170-181
    • Ronkina, N.1
  • 33
    • 0031952597 scopus 로고    scopus 로고
    • Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK
    • Dalby, K.N., Morrice, N., Caudwell, F.B., Avruch, J. & Cohen, P. Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK. J. Biol. Chem. 273, 1496-1505 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 1496-1505
    • Dalby, K.N.1    Morrice, N.2    Caudwell, F.B.3    Avruch, J.4    Cohen, P.5
  • 34
    • 0033578776 scopus 로고    scopus 로고
    • 90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1
    • Jensen, C.J. et al. 90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. J. Biol. Chem. 274, 27168-27176 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 27168-27176
    • Jensen, C.J.1
  • 35
    • 0034653608 scopus 로고    scopus 로고
    • The P13K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck, B. & Alessi, D.R. The P13K-PDK1 connection: More than just a road to PKB. Biochem. J. 346, 561-576 (2000).
    • (2000) Biochem. J , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 36
    • 0034747717 scopus 로고    scopus 로고
    • Altered extracellular signal-regulated kinase signaling and glycogen metabolism in skeletal muscle from p90 ribosomal S6 kinase 2 knockout mice
    • Dufresne, S.D. et al. Altered extracellular signal-regulated kinase signaling and glycogen metabolism in skeletal muscle from p90 ribosomal S6 kinase 2 knockout mice. Mol Cell Biol. 21, 81-87 (2001).
    • (2001) Mol Cell Biol , vol.21 , pp. 81-87
    • Dufresne, S.D.1
  • 37
    • 19744364796 scopus 로고    scopus 로고
    • Structural bioinformatics-based design of selective, irreversible kinase inhibitors
    • Cohen, M.S., Zhang, C., Shokat, K.M. & Taunton, J. Structural bioinformatics-based design of selective, irreversible kinase inhibitors. Science 308, 1318-1321 (2005).
    • (2005) Science , vol.308 , pp. 1318-1321
    • Cohen, M.S.1    Zhang, C.2    Shokat, K.M.3    Taunton, J.4
  • 38
    • 33846312875 scopus 로고    scopus 로고
    • B1-D1870 is a specific inhibitor of the p90 RSK (ribosomal S6 kinase) isoforms in vitro and in vivo
    • Sapkota, G.P. et al. B1-D1870 is a specific inhibitor of the p90 RSK (ribosomal S6 kinase) isoforms in vitro and in vivo. Biochem. J. 401, 29-38 (2007).
    • (2007) Biochem. J , vol.401 , pp. 29-38
    • Sapkota, G.P.1
  • 39
    • 13444270324 scopus 로고    scopus 로고
    • Identification of the first specific inhibitor of p90 ribosomal S6 kinase (RSK) reveals an unexpected role for RSK in cancer cell proliferation
    • Smith, J.A. et al. Identification of the first specific inhibitor of p90 ribosomal S6 kinase (RSK) reveals an unexpected role for RSK in cancer cell proliferation. Cancer Res. 65, 1027-1034 (2005).
    • (2005) Cancer Res , vol.65 , pp. 1027-1034
    • Smith, J.A.1
  • 40
    • 0031577164 scopus 로고    scopus 로고
    • Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk
    • Vik, T.A. & Ryder, J.W. Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk. Biochem. Biophys. Res. Commun. 235, 398-402 (1997).
    • (1997) Biochem. Biophys. Res. Commun , vol.235 , pp. 398-402
    • Vik, T.A.1    Ryder, J.W.2
  • 41
    • 0034667764 scopus 로고    scopus 로고
    • p38 map kinase substrate specificity differs greatly for protein and peptide substrates
    • Hawkins, J., Zheng, S., Frantz, B. & LoGrasso, P. p38 map kinase substrate specificity differs greatly for protein and peptide substrates. Arch. Biochem. Biophys. 382, 310-313 (2000).
    • (2000) Arch. Biochem. Biophys , vol.382 , pp. 310-313
    • Hawkins, J.1    Zheng, S.2    Frantz, B.3    LoGrasso, P.4
  • 42
    • 0036273201 scopus 로고    scopus 로고
    • Distinct cellular functions of MK2
    • Kotlyarov, A. et al. Distinct cellular functions of MK2. Mol. Cell. Biol. 22, 4827-4835 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4827-4835
    • Kotlyarov, A.1
  • 44
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and 1GF-1
    • Alessi, D.R. et al. Mechanism of activation of protein kinase B by insulin and 1GF-1. EMBO J. 15, 6541-6551 (1996).
    • (1996) EMBO J , vol.15 , pp. 6541-6551
    • Alessi, D.R.1
  • 45
    • 0035793574 scopus 로고    scopus 로고
    • p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • Rane, M.J. et al. p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J. Biol. Chem. 276, 3517-3523 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 3517-3523
    • Rane, M.J.1
  • 46
    • 34547588567 scopus 로고    scopus 로고
    • Hsp27 regulates Akt activation and PMN apoptosis by scaffolding MK2 to Akt signal complex
    • Wu, R. et al. Hsp27 regulates Akt activation and PMN apoptosis by scaffolding MK2 to Akt signal complex. J. Biol. Chem. 282, 21598-21608 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 21598-21608
    • Wu, R.1
  • 47
    • 33847042741 scopus 로고    scopus 로고
    • A clickable inhibitor reveals context-dependent autoactivation of p90 RSK
    • Cohen, M.S., Hadjivassiliou, H. & Taunton, J. A clickable inhibitor reveals context-dependent autoactivation of p90 RSK. Nat. Chem. Biol. 3, 156-160 (2007).
    • (2007) Nat. Chem. Biol , vol.3 , pp. 156-160
    • Cohen, M.S.1    Hadjivassiliou, H.2    Taunton, J.3
  • 48
    • 2442635429 scopus 로고    scopus 로고
    • Reciprocal CD40 signals through p38MAPK and ERK-1/2 induce counteracting immune responses
    • Mathur, R.K., Awasthi, A., Wadhone, P., Ramanamurthy, B. & Saha, B. Reciprocal CD40 signals through p38MAPK and ERK-1/2 induce counteracting immune responses. Nat Med. 10, 540-544 (2004).
    • (2004) Nat Med , vol.10 , pp. 540-544
    • Mathur, R.K.1    Awasthi, A.2    Wadhone, P.3    Ramanamurthy, B.4    Saha, B.5
  • 49
    • 0030767442 scopus 로고    scopus 로고
    • EGF induced SOS phosphorylation in PC12 cells involves P90 RSK-2
    • Douville, E. & Downward, J. EGF induced SOS phosphorylation in PC12 cells involves P90 RSK-2. Oncogene 15, 373-383 (1997).
    • (1997) Oncogene , vol.15 , pp. 373-383
    • Douville, E.1    Downward, J.2
  • 50
    • 23844516065 scopus 로고    scopus 로고
    • The Mnks are novel components in the control of TNF-α biosynthesis and phosphorylate and regulate hnRNP A1
    • Buxade, M. et al. The Mnks are novel components in the control of TNF-α biosynthesis and phosphorylate and regulate hnRNP A1. Immunity 23, 177-189 (2005).
    • (2005) Immunity , vol.23 , pp. 177-189
    • Buxade, M.1
  • 51
    • 0033575236 scopus 로고    scopus 로고
    • + exchanger isoform-1
    • + exchanger isoform-1. J. Biol. Chem. 274, 20206-20214 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 20206-20214
    • Takahashi, E.1
  • 52
    • 0024836461 scopus 로고
    • Distinct endocytatic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West, M.A., Bretscher, M.S. & Watts, C. Distinct endocytatic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell Biol. 109, 2731-2739 (1989).
    • (1989) J. Cell Biol , vol.109 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 53
    • 0029148878 scopus 로고
    • Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products
    • Sallusto, F., Cella, M., Danieli, C. & Lanzavecchia, A. Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products. J. Exp. Med. 182, 389-400 (1995).
    • (1995) J. Exp. Med , vol.182 , pp. 389-400
    • Sallusto, F.1    Cella, M.2    Danieli, C.3    Lanzavecchia, A.4
  • 54
    • 1642293247 scopus 로고    scopus 로고
    • Ribosomal S6 kinase (RSK) regulates phosphorylation of filamin A on an important regulatory site
    • Woo, M.S., Ohta, Y., Rabinovitz, I., Stossel, T.P. & Blenis, J. Ribosomal S6 kinase (RSK) regulates phosphorylation of filamin A on an important regulatory site. Mol. Cell. Biol. 24, 3025-3035 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3025-3035
    • Woo, M.S.1    Ohta, Y.2    Rabinovitz, I.3    Stossel, T.P.4    Blenis, J.5
  • 55
    • 0036193378 scopus 로고    scopus 로고
    • MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts
    • Wiggin, G.R. et al. MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts. Mol. Cell. Biol. 22, 2871-2881 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 2871-2881
    • Wiggin, G.R.1
  • 56
    • 33745837261 scopus 로고    scopus 로고
    • Differential regulafion of T-cell growth by IL-2 and IL-15
    • Cornish, G.H., Sinclair, L.V. & Cantrell, D.A. Differential regulafion of T-cell growth by IL-2 and IL-15. Blood 108, 600-608 (2006).
    • (2006) Blood , vol.108 , pp. 600-608
    • Cornish, G.H.1    Sinclair, L.V.2    Cantrell, D.A.3
  • 57
    • 0029099408 scopus 로고
    • Assay and expression of mitogen-activated protein kinase, MAP kinase kinase, and Raf
    • Alessi, D.R. et al. Assay and expression of mitogen-activated protein kinase, MAP kinase kinase, and Raf. Methods Enzymol. 255, 279-290 (1995).
    • (1995) Methods Enzymol , vol.255 , pp. 279-290
    • Alessi, D.R.1
  • 58
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S.P., Reddy, H., Caivano, M. & Cohen, P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105 (2000).
    • (2000) Biochem. J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.