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Volumn 119, Issue 8, 2006, Pages 1579-1591

TRAF6 activation of PI 3-kinase-dependent cytoskeletal changes is cooperative with Ras and is mediated by an interaction with cytoplasmic Src

Author keywords

BiFC Split GFP; Filopodia; IL 1 Toll receptor; Proteasome; Sequestosome

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 1; MYELOID DIFFERENTIATION FACTOR 88; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PROLINE; PROTEIN SH2; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; RAS PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6;

EID: 33646688235     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02889     Document Type: Article
Times cited : (33)

References (87)
  • 1
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S. and Takeda, K. (2004). Toll-like receptor signalling. Nat. Rev. Immunol. 4, 499-511.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 2
    • 0344196965 scopus 로고    scopus 로고
    • The interleukin 1 receptor: Ligand interactions and signal transduction
    • Auron, P. E. (1998). The interleukin 1 receptor: ligand interactions and signal transduction. Cytokine Growth Factor Rev. 9, 221-237.
    • (1998) Cytokine Growth Factor Rev. , vol.9 , pp. 221-237
    • Auron, P.E.1
  • 3
    • 21344463770 scopus 로고    scopus 로고
    • Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
    • Babu, J. R., Geetha, T. and Wooten, M. W. (2005). Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J. Neurochem. 94, 192-203.
    • (2005) J. Neurochem. , vol.94 , pp. 192-203
    • Babu, J.R.1    Geetha, T.2    Wooten, M.W.3
  • 4
    • 0033563101 scopus 로고    scopus 로고
    • Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain
    • Baud, V., Liu, Z. G., Bennett, B., Suzuki, N., Xia, Y. and Karin, M. (1999). Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. Genes Dev. 13, 1297-1308.
    • (1999) Genes Dev. , vol.13 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3    Suzuki, N.4    Xia, Y.5    Karin, M.6
  • 6
    • 0035896734 scopus 로고    scopus 로고
    • Differential signaling and tumor necrosis factor receptor-associated factor (TRAF) degradation mediated by CD40 and the Epstein-Barr virus oncoprotein latent membrane protein 1 (LMP1)
    • Brown, K. D., Hostager, B. S. and Bishop, G. A. (2001). Differential signaling and tumor necrosis factor receptor-associated factor (TRAF) degradation mediated by CD40 and the Epstein-Barr virus oncoprotein latent membrane protein 1 (LMP1). J. Exp. Med. 193, 943-954.
    • (2001) J. Exp. Med. , vol.193 , pp. 943-954
    • Brown, K.D.1    Hostager, B.S.2    Bishop, G.A.3
  • 7
    • 0029761275 scopus 로고    scopus 로고
    • TRAF6 is a signal transducer for interleukin-1
    • Cao, Z., Xiong, J., Takeuchi, M., Kurama, T. and Goeddel, D. V. (1996). TRAF6 is a signal transducer for interleukin-1. Nature 383, 443-446.
    • (1996) Nature , vol.383 , pp. 443-446
    • Cao, Z.1    Xiong, J.2    Takeuchi, M.3    Kurama, T.4    Goeddel, D.V.5
  • 8
    • 0034680767 scopus 로고    scopus 로고
    • Lack of palmitoylation redirects p59Hck from the plasma membrane to p61Hck-positive lysosomes
    • Carreno, S., Gouze, M. E., Schaak, S., Emorine, L. J. and Maridonneau-Parini, I. (2000). Lack of palmitoylation redirects p59Hck from the plasma membrane to p61Hck-positive lysosomes. J. Biol. Chem. 275, 36223-36229.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36223-36229
    • Carreno, S.1    Gouze, M.E.2    Schaak, S.3    Emorine, L.J.4    Maridonneau-Parini, I.5
  • 9
    • 0035794135 scopus 로고    scopus 로고
    • Ras controls tumor necrosis factor receptor-associated factor (TRAF)6-dependent induction of nuclear factor-kappa b. Selective regulation through receptor signaling components
    • Caunt, C. J., Kiss-Toth, E., Carlotti, F., Chapman, R. and Qwarnstrom, E. E. (2001). Ras controls tumor necrosis factor receptor-associated factor (TRAF)6-dependent induction of nuclear factor-kappa b. Selective regulation through receptor signaling components. J. Biol. Chem. 276, 6280-6288.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6280-6288
    • Caunt, C.J.1    Kiss-Toth, E.2    Carlotti, F.3    Chapman, R.4    Qwarnstrom, E.E.5
  • 10
    • 0038320263 scopus 로고    scopus 로고
    • The signaling adaptors and pathways activated by TNF superfamily
    • Dempsey, P. W., Doyle, S. E., He, J. Q. and Cheng, G. (2003). The signaling adaptors and pathways activated by TNF superfamily. Cytokine Growth Factor Rev. 14, 193-209.
    • (2003) Cytokine Growth Factor Rev. , vol.14 , pp. 193-209
    • Dempsey, P.W.1    Doyle, S.E.2    He, J.Q.3    Cheng, G.4
  • 12
    • 0037465251 scopus 로고    scopus 로고
    • The interleukin-1 receptor/Toll-like receptor superfamily: Signal transduction during inflammation and host defense
    • Dunne, A. and O'Neill, L. A. (2003). The interleukin-1 receptor/ Toll-like receptor superfamily: signal transduction during inflammation and host defense. Sci STKE
    • (2003) Sci. STKE
    • Dunne, A.1    O'Neill, L.A.2
  • 13
    • 0442325388 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis
    • Duran, A., Serrano, M., Leitges, M., Flores, J. M., Picard, S., Brown, J. P., Moscat, J. and Diaz-Meco, M. T. (2004). The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis. Dev. Cell 6, 303-309.
    • (2004) Dev. Cell , vol.6 , pp. 303-309
    • Duran, A.1    Serrano, M.2    Leitges, M.3    Flores, J.M.4    Picard, S.5    Brown, J.P.6    Moscat, J.7    Diaz-Meco, M.T.8
  • 14
    • 7444235791 scopus 로고    scopus 로고
    • TIFA activates IkappaB kinase (IKK) by promoting oligomerization and ubiquitination of TRAF6
    • Ea, C. K., Sun, L., Inoue, J. and Chen, Z. J. (2004). TIFA activates IkappaB kinase (IKK) by promoting oligomerization and ubiquitination of TRAF6. Proc. Natl. Acad. Sci. USA 101, 15318-15323.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15318-15323
    • Ea, C.K.1    Sun, L.2    Inoue, J.3    Chen, Z.J.4
  • 15
    • 0037449777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/ reoxygenation
    • Fan, C., Li, Q., Ross, D. and Engelhardt, J. F. (2003). Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/ reoxygenation. J. Biol. Chem. 278, 2072-2080.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2072-2080
    • Fan, C.1    Li, Q.2    Ross, D.3    Engelhardt, J.F.4
  • 16
    • 0034646632 scopus 로고    scopus 로고
    • Discrete signaling regions in the lymphotoxin-beta receptor for tumor necrosis factor receptor-associated factor binding, subcellular localization, and activation of cell death and NF-kappaB pathways
    • Force, W. R., Glass, A. A., Benedict, C. A., Cheung, T. C., Lama, J. and Ware, C. F. (2000). Discrete signaling regions in the lymphotoxin-beta receptor for tumor necrosis factor receptor-associated factor binding, subcellular localization, and activation of cell death and NF-kappaB pathways. J. Biol. Chem. 275, 11121-11129.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11121-11129
    • Force, W.R.1    Glass, A.A.2    Benedict, C.A.3    Cheung, T.C.4    Lama, J.5    Ware, C.F.6
  • 17
    • 0035100960 scopus 로고    scopus 로고
    • The role of TNF-receptor family members and other TRAF-dependent receptors in bone resorption
    • Gravallese, E. M., Galson, D. L., Goldring, S. R. and Auron, P. E. (2001). The role of TNF-receptor family members and other TRAF-dependent receptors in bone resorption. Arthritis Res. 3, 6-12.
    • (2001) Arthritis Res. , vol.3 , pp. 6-12
    • Gravallese, E.M.1    Galson, D.L.2    Goldring, S.R.3    Auron, P.E.4
  • 18
    • 0038719690 scopus 로고    scopus 로고
    • Membrane rafts play a crucial role in receptor activator of nuclear factor kappaB signaling and osteoclast function
    • Ha, H., Kwak, H. B., Lee, S. K., Na, D. S., Rudd, C. E., Lee, Z. H. and Kim, H. H. (2003). Membrane rafts play a crucial role in receptor activator of nuclear factor kappaB signaling and osteoclast function. J. Biol. Chem. 278, 18573-18580.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18573-18580
    • Ha, H.1    Kwak, H.B.2    Lee, S.K.3    Na, D.S.4    Rudd, C.E.5    Lee, Z.H.6    Kim, H.H.7
  • 19
    • 0034685914 scopus 로고    scopus 로고
    • Recruitment of CD40 and tumor necrosis factor receptor-associated factors 2 and 3 to membrane microdomains during CD40 signaling
    • Hostager, B. S., Catlett, I. M. and Bishop, G. A. (2000). Recruitment of CD40 and tumor necrosis factor receptor-associated factors 2 and 3 to membrane microdomains during CD40 signaling. J. Biol. Chem. 275, 15392-15398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15392-15398
    • Hostager, B.S.1    Catlett, I.M.2    Bishop, G.A.3
  • 20
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y. and Kerppola, T. K. (2002a). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 21
    • 0037090315 scopus 로고    scopus 로고
    • Regulation of IL-1 receptor-associated kinases by lipopolysaccharide
    • Hu, J., Jacinto, R., McCall, C. and Li, L. (2002b). Regulation of IL-1 receptor-associated kinases by lipopolysaccharide. J. Immunol. 168, 3910-3914.
    • (2002) J. Immunol. , vol.168 , pp. 3910-3914
    • Hu, J.1    Jacinto, R.2    McCall, C.3    Li, L.4
  • 22
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • James, S. R., Downes, C. P., Gigg, R., Grove, S. J., Holmes, A. B. and Alessi, D. R. (1996). Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation. Biochem. J. 315, 709-713.
    • (1996) Biochem. J. , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.4    Holmes, A.B.5    Alessi, D.R.6
  • 23
  • 24
    • 0141682703 scopus 로고    scopus 로고
    • Ubiquitin activated tumor necrosis factor receptor associated factor-6 (TRAF6) is recycled via deubiquitination
    • Jensen, L. E. and Whitehead, A. S. (2003). Ubiquitin activated tumor necrosis factor receptor associated factor-6 (TRAF6) is recycled via deubiquitination. FEBS Lett. 553, 190-194.
    • (2003) FEBS Lett. , vol.553 , pp. 190-194
    • Jensen, L.E.1    Whitehead, A.S.2
  • 25
    • 0031729612 scopus 로고    scopus 로고
    • Expression of Src family kinases and their putative substrates in the human preosteoclastic cell line FLG 29.1
    • Jeschke, M., Brandi, M. L. and Susa, M. (1998). Expression of Src family kinases and their putative substrates in the human preosteoclastic cell line FLG 29.1. J. Bone Miner. Res. 13, 1880-1889.
    • (1998) J. Bone Miner. Res. , vol.13 , pp. 1880-1889
    • Jeschke, M.1    Brandi, M.L.2    Susa, M.3
  • 27
    • 0038578823 scopus 로고    scopus 로고
    • The PI-3 kinase/Akt pathway and T cell activation: Pleiotropic pathways downstream of PIP3
    • Kane, L. P. and Weiss, A. (2003). The PI-3 kinase/Akt pathway and T cell activation: pleiotropic pathways downstream of PIP3. Immunol. Rev. 192, 7-20.
    • (2003) Immunol. Rev. , vol.192 , pp. 7-20
    • Kane, L.P.1    Weiss, A.2
  • 28
    • 2142646543 scopus 로고    scopus 로고
    • A proline-rich motif in the C terminus of Akt contributes to its localization in the immunological synapse
    • Kane, L. P., Mollenauer, M. N. and Weiss, A. (2004). A proline-rich motif in the C terminus of Akt contributes to its localization in the immunological synapse. J. Immunol. 172, 5441-5449.
    • (2004) J. Immunol. , vol.172 , pp. 5441-5449
    • Kane, L.P.1    Mollenauer, M.N.2    Weiss, A.3
  • 29
    • 0037966408 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase activity leads to silica-induced NF-kappaB activation through interacting with tyrosine-phosphorylated I(kappa)B-alpha and contributing to tyrosine phosphorylation of p65 NF-kappaB
    • Kang, J. L., Lee, H. S., Pack, I. S., Hur, K. C. and Castranova, V. (2003). Phosphoinositide 3-kinase activity leads to silica-induced NF-kappaB activation through interacting with tyrosine-phosphorylated I(kappa)B-alpha and contributing to tyrosine phosphorylation of p65 NF-kappaB. Mol. Cell. Biochem. 248, 17-24.
    • (2003) Mol. Cell. Biochem. , vol.248 , pp. 17-24
    • Kang, J.L.1    Lee, H.S.2    Pack, I.S.3    Hur, K.C.4    Castranova, V.5
  • 30
    • 0035868884 scopus 로고    scopus 로고
    • Segregation of TRAF6-mediated signaling pathways clarifies its role in osteoclastogenesis
    • Kobayashi, N., Kadono, Y., Naito, A., Matsumoto, K., Yamamoto, T., Tanaka, S. and Inoue, J. (2001). Segregation of TRAF6-mediated signaling pathways clarifies its role in osteoclastogenesis. EMBO J. 20, 1271-1280.
    • (2001) EMBO J. , vol.20 , pp. 1271-1280
    • Kobayashi, N.1    Kadono, Y.2    Naito, A.3    Matsumoto, K.4    Yamamoto, T.5    Tanaka, S.6    Inoue, J.7
  • 31
    • 0033567388 scopus 로고    scopus 로고
    • ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway
    • Kopp, E., Medzhitov, R., Carothers, J., Xiao, C., Douglas, I., Janeway, C. A. and Ghosh, S. (1999). ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Genes Dev. 13, 2059-2071.
    • (1999) Genes Dev. , vol.13 , pp. 2059-2071
    • Kopp, E.1    Medzhitov, R.2    Carothers, J.3    Xiao, C.4    Douglas, I.5    Janeway, C.A.6    Ghosh, S.7
  • 32
    • 11944268320 scopus 로고    scopus 로고
    • SQSTM and Paget's disease of bone
    • Layfield, R. and Hocking, L. J. (2004). SQSTM and Paget's disease of bone. Calcif. Tissue Int. 75, 347-357.
    • (2004) Calcif. Tissue Int. , vol.75 , pp. 347-357
    • Layfield, R.1    Hocking, L.J.2
  • 33
    • 1642358911 scopus 로고    scopus 로고
    • Cytoplasmic domain-mediated dimerizations of toll-like receptor 4 observed by beta -lactamase enzyme fragment complementation
    • Lee, H. K., Dunzendorfer, S. and Tobias, P. S. (2004a). Cytoplasmic domain-mediated dimerizations of toll-like receptor 4 observed by beta -lactamase enzyme fragment complementation. J. Biol. Chem. 279, 10564-10574.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10564-10574
    • Lee, H.K.1    Dunzendorfer, S.2    Tobias, P.S.3
  • 34
    • 3543028591 scopus 로고    scopus 로고
    • FGF-2 induced by interleukin-1 beta through the action of phosphatidylinositol 3-kinase mediates endothelial mesenchymal transformation in corneal endothelial cells
    • Lee, H. T., Leeg J. G., Na, M. and Kay, E. P. (2004b). FGF-2 induced by interleukin-1 beta through the action of phosphatidylinositol 3-kinase mediates endothelial mesenchymal transformation in corneal endothelial cells. J. Biol. Chem. 279, 32325-32332.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32325-32332
    • Lee, H.T.1    Leeg, J.G.2    Na, M.3    Kay, E.P.4
  • 35
    • 15944410614 scopus 로고    scopus 로고
    • PDKI nucleates T cell receptor-induced signaling complex for NF-kappaB activation
    • Lee, K. Y., D'Acquisto, F., Hayden, M. S., Shim, J. H. and Ghosh, S. (2005). PDKI nucleates T cell receptor-induced signaling complex for NF-kappaB activation. Science 308, 114-118.
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.Y.1    D'Acquisto, F.2    Hayden, M.S.3    Shim, J.H.4    Ghosh, S.5
  • 37
    • 0034725584 scopus 로고    scopus 로고
    • Characterization of interleukin-1 receptor-associated kinase in normal and endotoxin-tolerant cells
    • Li, L., Consart, S., Hu, J. and McCall, C. E. (2000). Characterization of interleukin-1 receptor-associated kinase in normal and endotoxin-tolerant cells. J. Biol. Chem. 275, 23340-23345.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23340-23345
    • Li, L.1    Consart, S.2    Hu, J.3    McCall, C.E.4
  • 38
    • 0025820850 scopus 로고
    • Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization
    • Lock, P., Ralph, S., Stanley, E., Boulet, L, Ramsay, R. and Dunn, A. R. (1991). Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization. Mol. Cell. Biol. 11, 4363-4370.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4363-4370
    • Lock, P.1    Ralph, S.2    Stanley, E.3    Boulet, L.4    Ramsay, R.5    Dunn, A.R.6
  • 39
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley, R. M., Killeen, N. and Lenardo, M. J. (2001). The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104, 487-501.
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 40
    • 0030067201 scopus 로고    scopus 로고
    • Deficiency of the Hck and Src tyrosine kinases results in extreme levels of extramedullary hematopoiesis
    • Lowell, C. A., Niwa, M., Soriano, P. and Varmus, H. E. (1996). Deficiency of the Hck and Src tyrosine kinases results in extreme levels of extramedullary hematopoiesis. Blood 87, 1780-1792.
    • (1996) Blood , vol.87 , pp. 1780-1792
    • Lowell, C.A.1    Niwa, M.2    Soriano, P.3    Varmus, H.E.4
  • 41
    • 23744456586 scopus 로고    scopus 로고
    • The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex
    • Luo, J., Field, S. J., Lee, J. Y., Engelman, J. A. and Cantley, L. C. (2005). The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex. J. Cell Biol. 170, 455-464.
    • (2005) J. Cell Biol. , vol.170 , pp. 455-464
    • Luo, J.1    Field, S.J.2    Lee, J.Y.3    Engelman, J.A.4    Cantley, L.C.5
  • 42
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the Re1A/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38
    • Madrid, L. V., Mayo, M. W., Reuther, J. Y. and Baldwin, A. S., Jr (2001). Akt stimulates the transactivation potential of the Re1A/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38. J. Biol. Chem. 276, 18934-18940.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin Jr., A.S.4
  • 45
    • 0037040883 scopus 로고    scopus 로고
    • Ras participates in the activation of p38 MAPK by interleukin-1 by associating with IRAK, IRAK2, TRAF6, and TAK-1
    • McDermott, E. P. and O'Neill, L. A. (2002). Ras participates in the activation of p38 MAPK by interleukin-1 by associating with IRAK, IRAK2, TRAF6, and TAK-1. J. Biol. Chem. 277, 7808-7815.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7808-7815
    • McDermott, E.P.1    O'Neill, L.A.2
  • 46
    • 0034043956 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: Dysregulation of cytokine, chemokine, and toll-like receptor 2 and 4 gene expression
    • Medvedev, A. E., Kopydlowski, K. M. and Vogel, S. N. (2000). Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: dysregulation of cytokine, chemokine, and toll-like receptor 2 and 4 gene expression. J. Immunol. 164, 5564-5574.
    • (2000) J. Immunol. , vol.164 , pp. 5564-5574
    • Medvedev, A.E.1    Kopydlowski, K.M.2    Vogel, S.N.3
  • 48
    • 0035424708 scopus 로고    scopus 로고
    • Exploring protein interactions by interaction-induced folding of proteins from complementary peptide fragments
    • Michnick, S. W. (2001). Exploring protein interactions by interaction-induced folding of proteins from complementary peptide fragments. Curr. Opin. Struct. Biol. 11, 472-477.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 472-477
    • Michnick, S.W.1
  • 49
    • 2642579936 scopus 로고    scopus 로고
    • Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex
    • Millard, T. H., Sharp, S. J. and Machesky, L. M. (2004). Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex. Biochem. J. 380, 1-17.
    • (2004) Biochem. J. , vol.380 , pp. 1-17
    • Millard, T.H.1    Sharp, S.J.2    Machesky, L.M.3
  • 50
    • 0034743875 scopus 로고    scopus 로고
    • Regulation and role of the atypical PKC isoforms in cell survival during tumor transformation
    • Moscat, J., Sanz, L., Sanchez, P. and Diaz-Meco, M. T. (2001). Regulation and role of the atypical PKC isoforms in cell survival during tumor transformation. Adv. Enzyme Regul. 41, 99-120.
    • (2001) Adv. Enzyme Regul. , vol.41 , pp. 99-120
    • Moscat, J.1    Sanz, L.2    Sanchez, P.3    Diaz-Meco, M.T.4
  • 53
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappaB activation by tumour necrosis factor requires the Akt scrine-threonine kinase
    • Ozes, O. N., Mayo, L. D., Gustin, J. A., Pfeffer, S. R., Pfeffer, L. M. and Donner, D. B. (1999). NF-kappaB activation by tumour necrosis factor requires the Akt scrine-threonine kinase. Nature 401, 82-85.
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 55
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park, Y. C., Burkitt, V., Villa, A. R., Tong, L. and Wu, H. (1999). Structural basis for self-association and receptor recognition of human TRAF2. Nature 398, 533-538.
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 56
    • 0030911597 scopus 로고    scopus 로고
    • Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein
    • Puls, A., Schmidt, S., Grawe, F. and Stabel, S. (1997). Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein. Proc. Natl. Acad. Sci. USA 94, 6191-6196.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6191-6196
    • Puls, A.1    Schmidt, S.2    Grawe, F.3    Stabel, S.4
  • 57
    • 0032841725 scopus 로고    scopus 로고
    • Activation of the small GTPase Cdc42 by the inflammatory cytokines TNF(alpha) and IL-1 and by the Epstein-Barr virus transforming protein LMP1
    • Puls, A., Eliopoulos, A. G., Nobes, C. D., Bridges, T., Young, L. S. and Hall, A. (1999). Activation of the small GTPase Cdc42 by the inflammatory cytokines TNF(alpha) and IL-1 and by the Epstein-Barr virus transforming protein LMP1. J. Cell Sci. 112, 2983-2992.
    • (1999) J. Cell Sci. , vol.112 , pp. 2983-2992
    • Puls, A.1    Eliopoulos, A.G.2    Nobes, C.D.3    Bridges, T.4    Young, L.S.5    Hall, A.6
  • 58
    • 0030695187 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase in interleukin 1 signaling. Physical interaction with the interleukin 1 receptor and requirement in NFκB and AP-1 activation
    • Reddy, S. A. G., Huang, J. H. and Liao, W. S. L. (1997). Phosphatidylinositol 3-kinase in interleukin 1 signaling. Physical interaction with the interleukin 1 receptor and requirement in NFκB and AP-1 activation. J. Biol. Chem. 272, 29167-29173.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29167-29173
    • Reddy, S.A.G.1    Huang, J.H.2    Liao, W.S.L.3
  • 59
    • 3543083870 scopus 로고    scopus 로고
    • The co-workers of actin filaments: From cell structures to signals
    • Revenu, C., Athman, R., Robine, S. and Louvard, D. (2004). The co-workers of actin filaments: from cell structures to signals. Nat. Rev. Mol. Cell Biol. 5, 635-646.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 635-646
    • Revenu, C.1    Athman, R.2    Robine, S.3    Louvard, D.4
  • 61
    • 12344318370 scopus 로고    scopus 로고
    • RhoA GTPase regulates B cell receptor signaling
    • Saci, A. and Carpenter, C. L. (2005). RhoA GTPase regulates B cell receptor signaling. Mol. Cell 17, 205-214.
    • (2005) Mol. Cell , vol.17 , pp. 205-214
    • Saci, A.1    Carpenter, C.L.2
  • 63
    • 0031946369 scopus 로고    scopus 로고
    • Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62
    • Sanchez, P., De Career, G., Sandoval, I. V., Moscat, J. and Diaz-Meco, M. T. (1998). Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol. Cell. Biol. 18, 3069-3080.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3069-3080
    • Sanchez, P.1    De Career, G.2    Sandoval, I.V.3    Moscat, J.4    Diaz-Meco, M.T.5
  • 65
    • 0034599476 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-l-TRAF6 pathway
    • Sanz, L., Diaz-Meco, M. T., Nakano, H. and Muscat, J. (2000). The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-l-TRAF6 pathway. EMBO J. 19, 1576-1586.
    • (2000) EMBO J. , vol.19 , pp. 1576-1586
    • Sanz, L.1    Diaz-Meco, M.T.2    Nakano, H.3    Muscat, J.4
  • 66
  • 67
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., Roth, M. G. and Simons, K. (1997). Interaction of influenza virus haemagglutinin with 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
  • 68
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener, M. L., Balm, J. R., Geetha, T., Wongg H. C., Krishna, N. R. and Wooten, M. W. (2004). Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol. 24, 8055-8068.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Balm, J.R.2    Geetha, T.3    Wongg, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 69
    • 0028835253 scopus 로고
    • A peptidomimetic inhibitor of farnesyl: Protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines
    • Sepp-Lorenzino, L., Ma. Z., Rands, E., Kohl, N. E., Gibbs, J. B., Oliff, A. and Rosen, N. (1995). A peptidomimetic inhibitor of farnesyl:protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines. Cancer Res. 55, 5302-5309.
    • (1995) Cancer Res. , vol.55 , pp. 5302-5309
    • Sepp-Lorenzino, L.1    Ma, Z.2    Rands, E.3    Kohl, N.E.4    Gibbs, J.B.5    Oliff, A.6    Rosen, N.7
  • 70
    • 0033038491 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-kappaB p65/RelA subunit
    • Sizemore, N., Leung, S. and Stark, G. R. (1999). Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-kappaB p65/RelA subunit. Mol. Cell, Biol. 19, 4798-4805.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4798-4805
    • Sizemore, N.1    Leung, S.2    Stark, G.R.3
  • 71
    • 1642379541 scopus 로고    scopus 로고
    • Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling
    • Storz, P., Doppler, H. and Toker, A. (2004). Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling. Mol. Cell. Biol. 24, 2614-2626.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2614-2626
    • Storz, P.1    Doppler, H.2    Toker, A.3
  • 73
    • 0035099717 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) receptor-associated kinase leads to activation of TAK1 by inducing TAB2 translocation in the IL-1 signaling pathway
    • Takaesu, G., Ninomiya-Tsuji, J., Kishida, S., Li, X., Stark, G. R. and Matsumoto, K. (2001). Interleukin-1 (IL-1) receptor-associated kinase leads to activation of TAK1 by inducing TAB2 translocation in the IL-1 signaling pathway. Mol. Cell. Biol. 21, 2475-2484.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2475-2484
    • Takaesu, G.1    Ninomiya-Tsuji, J.2    Kishida, S.3    Li, X.4    Stark, G.R.5    Matsumoto, K.6
  • 74
    • 0038526352 scopus 로고    scopus 로고
    • Identification of TIFA as an adapter protein that links tumor necrosis factor receptor-associated factor 6 (TRAF6) to interleukin-1 (IL-1) receptor-associated kinase-1 (INAK-1) in IL-1 receptor signaling
    • Takatsuna, H., Kato, H., Gohda, J., Akiyama, T., Moriya, A., Okamoto, Y., Yamagata, Y., Otsuka, M., Umezawa, K., Semba, K. et al. (2003). Identification of TIFA as an adapter protein that links tumor necrosis factor receptor-associated factor 6 (TRAF6) to interleukin-1 (IL-1) receptor-associated kinase-1 (INAK-1) in IL-1 receptor signaling. J. Biol. Chem. 278, 12144-12150.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12144-12150
    • Takatsuna, H.1    Kato, H.2    Gohda, J.3    Akiyama, T.4    Moriya, A.5    Okamoto, Y.6    Yamagata, Y.7    Otsuka, M.8    Umezawa, K.9    Semba, K.10
  • 75
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A. and Mosialos, G. (2003). CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members, Nature 424, 793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 77
    • 4644300280 scopus 로고    scopus 로고
    • Regulation and cellular roles of phosphoinositide 5-kinases
    • Weernink, P. A. O., Schmidt, M. and Jakobs, K. H. (2004). Regulation and cellular roles of phosphoinositide 5-kinases. Eur. J. Pharmacol. 500, 87-99.
    • (2004) Eur. J. Pharmacol. , vol.500 , pp. 87-99
    • Weernink, P.A.O.1    Schmidt, M.2    Jakobs, K.H.3
  • 78
    • 0033393957 scopus 로고    scopus 로고
    • TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src
    • Wong, B. R., Besser, D., Kim, N., Arron, J. R., Vologodskaia, M., Hanafusa, H. and Choi, Y. (1999). TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src. Mol. Cell 4, 1041-1049.
    • (1999) Mol. Cell , vol.4 , pp. 1041-1049
    • Wong, B.R.1    Besser, D.2    Kim, N.3    Arron, J.R.4    Vologodskaia, M.5    Hanafusa, H.6    Choi, Y.7
  • 79
    • 2442536091 scopus 로고    scopus 로고
    • The TRAF6 RING finger domain mediates physical interaction with Ubc13
    • Wooff, J., Pastushok, L., Hanna, M., Fu, Y. and Xiao, W. (2004). The TRAF6 RING finger domain mediates physical interaction with Ubc13. FEBS Lett. 566, 229-233.
    • (2004) FEBS Lett. , vol.566 , pp. 229-233
    • Wooff, J.1    Pastushok, L.2    Hanna, M.3    Fu, Y.4    Xiao, W.5
  • 80
    • 0035896518 scopus 로고    scopus 로고
    • The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor
    • Wooten, M. W., Seibenhener, M. L., Mamidipudi, V., Diaz-Meco, M. T., Barker, P. A. and Muscat, J. (2001). The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. J. Biol. Chem. 276, 7709-7712.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7709-7712
    • Wooten, M.W.1    Seibenhener, M.L.2    Mamidipudi, V.3    Diaz-Meco, M.T.4    Barker, P.A.5    Muscat, J.6
  • 81
    • 27444433045 scopus 로고    scopus 로고
    • The p62 scaffold regulates NGF-induced NF-kappa B activation by influencing TRAF6 polyubiquitination
    • Wooten, M. W., Geetha, T., Seibenhener, M. L., Lewis, M. S., Bobu, J. R., Diaz-Meco, M. T. and Moscat, J. (2005). The p62 scaffold regulates NGF-induced NF-kappa B activation by influencing TRAF6 polyubiquitination. J. Biol. Chem. 280, 35625-35629.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35625-35629
    • Wooten, M.W.1    Geetha, T.2    Seibenhener, M.L.3    Lewis, M.S.4    Bobu, J.R.5    Diaz-Meco, M.T.6    Moscat, J.7
  • 82
    • 0035862994 scopus 로고    scopus 로고
    • Genetic evidence for a role for Src family kinases in TNF family receptor signaling and cell survival
    • Xing, L., Venegas, A. M., Chen, A., Garrett-Beal, L., Boyce, B. F., Varmus, H. E. and Schwartzberg, P. L. (2001). Genetic evidence for a role for Src family kinases in TNF family receptor signaling and cell survival. Genes Dev. 15, 241-253.
    • (2001) Genes Dev. , vol.15 , pp. 241-253
    • Xing, L.1    Venegas, A.M.2    Chen, A.3    Garrett-Beal, L.4    Boyce, B.F.5    Varmus, H.E.6    Schwartzberg, P.L.7
  • 83
    • 0030868909 scopus 로고    scopus 로고
    • The interleukin-1 receptor-associated kinase is degraded by proteosomes following its phosphorylation
    • Yamin, T.-T. and Miller, D. K. (1997). The interleukin-1 receptor-associated kinase is degraded by proteosomes following its phosphorylation. J. Biol. Chem. 272, 21540-21547.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21540-21547
    • Yamin, T.-T.1    Miller, D.K.2
  • 86
    • 0345826123 scopus 로고    scopus 로고
    • Interleukin 1 activates STAT3/nuclear factor-kappaB cross-talk via a unique TRAF6- and p65-dependent mechanism
    • Yoshida, Y., Kumar, A., Koyama, Y., Peng, H., Arman, A., Boch, J. A. and Auron, P. E. (2004). Interleukin 1 activates STAT3/nuclear factor-kappaB cross-talk via a unique TRAF6- and p65-dependent mechanism. J. Biol. Chem. 279, 1768-1776.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1768-1776
    • Yoshida, Y.1    Kumar, A.2    Koyama, Y.3    Peng, H.4    Arman, A.5    Boch, J.A.6    Auron, P.E.7
  • 87
    • 0035968303 scopus 로고    scopus 로고
    • A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains
    • Zapata, J. M., Pawlowski, K., Haas, E., Ware, C. F., Godzik, A. and Reed, J. C. (2001). A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains. J. Biol. Chem. 276, 24242-24252.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24242-24252
    • Zapata, J.M.1    Pawlowski, K.2    Haas, E.3    Ware, C.F.4    Godzik, A.5    Reed, J.C.6


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