메뉴 건너뛰기




Volumn 580, Issue 21, 2006, Pages 5023-5028

Theileria-induced constitutive IKK activation is independent of functional Hsp90

Author keywords

Cancer; Chaperone; Parasite; Signal transduction; Transformation

Indexed keywords

ANSAMYCIN DERIVATIVE; BENZOQUINONE; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SYNAPTOTAGMIN;

EID: 33748334342     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.08.020     Document Type: Article
Times cited : (6)

References (41)
  • 1
    • 0024378639 scopus 로고
    • Infection with the intracellular protozoan parasite Theileria parva induces constitutively high levels of NF-κB in bovine T lymphocytes
    • Ivanov V., Stein B., Baumann I., Dobbelaere D.A., Herrlich P., and Williams R.O. Infection with the intracellular protozoan parasite Theileria parva induces constitutively high levels of NF-κB in bovine T lymphocytes. Mol. Cell. Biol. 9 (1989) 4677-4686
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4677-4686
    • Ivanov, V.1    Stein, B.2    Baumann, I.3    Dobbelaere, D.A.4    Herrlich, P.5    Williams, R.O.6
  • 4
    • 0043094284 scopus 로고    scopus 로고
    • Theileria parva-transformed T cells show enhanced resistance to Fas/Fas ligand-induced apoptosis
    • Kuenzi P., Schneider P., and Dobbelaere D.A. Theileria parva-transformed T cells show enhanced resistance to Fas/Fas ligand-induced apoptosis. J. Immunol. 171 (2003) 1224-1231
    • (2003) J. Immunol. , vol.171 , pp. 1224-1231
    • Kuenzi, P.1    Schneider, P.2    Dobbelaere, D.A.3
  • 5
    • 3042774136 scopus 로고    scopus 로고
    • The strategies of the Theileria parasite: a new twist in host-pathogen interactions
    • Dobbelaere D.A., and Kuenzi P. The strategies of the Theileria parasite: a new twist in host-pathogen interactions. Curr. Opin. Immunol. 16 (2004) 524-530
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 524-530
    • Dobbelaere, D.A.1    Kuenzi, P.2
  • 6
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden M.S., and Ghosh S. Signaling to NF-κB. Genes Dev. 18 (2004) 2195-2224
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 7
    • 0033996762 scopus 로고    scopus 로고
    • The IκB kinase (IKK) and NF-κB: key elements of proinflammatory signalling
    • Karin M., and Delhase M. The IκB kinase (IKK) and NF-κB: key elements of proinflammatory signalling. Semin. Immunol. 12 (2000) 85-98
    • (2000) Semin. Immunol. , vol.12 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 9
    • 1642553460 scopus 로고    scopus 로고
    • To be, or not to be: NF-κB is the answer - role of Rel/NF-κB in the regulation of apoptosis
    • Kucharczak J., Simmons M.J., Fan Y., and Gelinas C. To be, or not to be: NF-κB is the answer - role of Rel/NF-κB in the regulation of apoptosis. Oncogene 22 (2003) 8961-8982
    • (2003) Oncogene , vol.22 , pp. 8961-8982
    • Kucharczak, J.1    Simmons, M.J.2    Fan, Y.3    Gelinas, C.4
  • 10
    • 33645999706 scopus 로고    scopus 로고
    • NF-κB and IKK as therapeutic targets in cancer
    • Kim H.J., Hawke N., and Baldwin A.S. NF-κB and IKK as therapeutic targets in cancer. Cell Death Differ. 13 (2006) 738-747
    • (2006) Cell Death Differ. , vol.13 , pp. 738-747
    • Kim, H.J.1    Hawke, N.2    Baldwin, A.S.3
  • 11
    • 25844459154 scopus 로고    scopus 로고
    • NF-κB: linking inflammation and immunity to cancer development and progression
    • Karin M., and Greten F.R. NF-κB: linking inflammation and immunity to cancer development and progression. Nat. Rev. Immunol. 5 (2005) 749-759
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 12
    • 0036828976 scopus 로고    scopus 로고
    • Hijacking of host cell IKK signalosomes by the transforming parasite Theileria
    • Heussler V.T., et al. Hijacking of host cell IKK signalosomes by the transforming parasite Theileria. Science 298 (2002) 1033-1036
    • (2002) Science , vol.298 , pp. 1033-1036
    • Heussler, V.T.1
  • 13
  • 14
    • 0035021123 scopus 로고    scopus 로고
    • The α and β subunits of IκB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF
    • Devin A., Lin Y., Yamaoka S., Li Z., Karin M., and Liu Z. The α and β subunits of IκB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol. Cell. Biol. 21 (2001) 3986-3994
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3986-3994
    • Devin, A.1    Lin, Y.2    Yamaoka, S.3    Li, Z.4    Karin, M.5    Liu, Z.6
  • 15
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh S., and Karin M. Missing pieces in the NF-κB puzzle. Cell 109 Suppl. (2002) S81-S96
    • (2002) Cell , vol.109 , Issue.SUPPL
    • Ghosh, S.1    Karin, M.2
  • 16
    • 0036728106 scopus 로고    scopus 로고
    • Chaperones and transcriptional regulation by nuclear receptors
    • Young J.C., and Hartl F.U. Chaperones and transcriptional regulation by nuclear receptors. Nat. Struct. Biol. 9 (2002) 640-642
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 640-642
    • Young, J.C.1    Hartl, F.U.2
  • 17
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman B.C., and Yamamoto K.R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296 (2002) 2232-2235
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 18
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: chaperoning signal transduction
    • Richter K., and Buchner J. Hsp90: chaperoning signal transduction. J. Cell. Physiol. 188 (2001) 281-290
    • (2001) J. Cell. Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 19
    • 1542328907 scopus 로고    scopus 로고
    • Inhibition of Hsp90: a new strategy for inhibiting protein kinases
    • Sreedhar A.S., Soti C., and Csermely P. Inhibition of Hsp90: a new strategy for inhibiting protein kinases. Biochim. Biophys. Acta 1697 (2004) 233-242
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 233-242
    • Sreedhar, A.S.1    Soti, C.2    Csermely, P.3
  • 20
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E.G., De Costa B., Myers C.E., and Neckers L.M. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91 (1994) 8324-8328
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 21
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte T.W., Blagosklonny M.V., Ingui C., and Neckers L. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 270 (1995) 24585-24588
    • (1995) J. Biol. Chem. , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 22
    • 0036187476 scopus 로고    scopus 로고
    • TNF-Induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol
    • Chen G., Cao P., and Goeddel D.V. TNF-Induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol. Cell 9 (2002) 401-410
    • (2002) Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 23
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L., and Lindquist S.L. HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5 (2005) 761-772
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 24
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs J.S., Xu W., and Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3 (2003) 213-217
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 25
    • 3142719113 scopus 로고    scopus 로고
    • Requirement of Hsp90 activity for IκB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-κB activation
    • Broemer M., Krappmann D., and Scheidereit C. Requirement of Hsp90 activity for IκB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-κB activation. Oncogene 23 (2004) 5378-5386
    • (2004) Oncogene , vol.23 , pp. 5378-5386
    • Broemer, M.1    Krappmann, D.2    Scheidereit, C.3
  • 26
    • 0025613824 scopus 로고
    • Expression of Tac antigen component of bovine interleukin-2 receptor in different leukocyte populations infected with Theileria parva or Theileria annulata
    • Dobbelaere D.A.E., et al. Expression of Tac antigen component of bovine interleukin-2 receptor in different leukocyte populations infected with Theileria parva or Theileria annulata. Infect. Immun. 58 (1990) 3847-3855
    • (1990) Infect. Immun. , vol.58 , pp. 3847-3855
    • Dobbelaere, D.A.E.1
  • 27
    • 0034958004 scopus 로고    scopus 로고
    • Theileria annulata: identification, by differential mRNA display, of modulated host and parasite gene expression in cell lines that are competent or attenuated for differentiation to the merozoite
    • Oura C.A., Tait A., and Shiels B.R. Theileria annulata: identification, by differential mRNA display, of modulated host and parasite gene expression in cell lines that are competent or attenuated for differentiation to the merozoite. Exp. Parasitol. 98 (2001) 10-19
    • (2001) Exp. Parasitol. , vol.98 , pp. 10-19
    • Oura, C.A.1    Tait, A.2    Shiels, B.R.3
  • 28
    • 0033623297 scopus 로고    scopus 로고
    • Characterisation of NF-κB complexes in Theileria parva-transformed T cells
    • Machado Jr. J., Fernandez P.C., Baumann I., and Dobbelaere D.A. Characterisation of NF-κB complexes in Theileria parva-transformed T cells. Microbes Infect. 2 (2000) 1311-1320
    • (2000) Microbes Infect. , vol.2 , pp. 1311-1320
    • Machado Jr., J.1    Fernandez, P.C.2    Baumann, I.3    Dobbelaere, D.A.4
  • 29
    • 0034870446 scopus 로고    scopus 로고
    • The Akt/PKB pathway is constitutively activated in Theileria-transformed leucocytes, but does not directly control constitutive NF-κB activation
    • Heussler V.T., Kuenzi P., Fraga F., Schwab R.A., Hemmings B.A., and Dobbelaere D.A. The Akt/PKB pathway is constitutively activated in Theileria-transformed leucocytes, but does not directly control constitutive NF-κB activation. Cell. Microbiol. 3 (2001) 537-550
    • (2001) Cell. Microbiol. , vol.3 , pp. 537-550
    • Heussler, V.T.1    Kuenzi, P.2    Fraga, F.3    Schwab, R.A.4    Hemmings, B.A.5    Dobbelaere, D.A.6
  • 30
    • 0021211620 scopus 로고
    • Do general anaesthetics act by competitive binding to specific receptors?
    • Franks N.P., and Lieb W.R. Do general anaesthetics act by competitive binding to specific receptors?. Nature 310 (1984) 599-601
    • (1984) Nature , vol.310 , pp. 599-601
    • Franks, N.P.1    Lieb, W.R.2
  • 31
    • 0032589462 scopus 로고    scopus 로고
    • IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H., Chiba H., Miyoshi H., Sugita T., and Toriumi W. IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain. J. Biol. Chem. 274 (1999) 30353-30356
    • (1999) J. Biol. Chem. , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 32
    • 2442429408 scopus 로고    scopus 로고
    • Transient and selective NF-κB p65 serine 536 phosphorylation induced by T cell costimulation is mediated by IκB kinase β and controls the kinetics of p65 nuclear import
    • Mattioli I., Sebald A., Bucher C., Charles R.P., Nakano H., Doi T., Kracht M., and Schmitz M.L. Transient and selective NF-κB p65 serine 536 phosphorylation induced by T cell costimulation is mediated by IκB kinase β and controls the kinetics of p65 nuclear import. J. Immunol. 172 (2004) 6336-6344
    • (2004) J. Immunol. , vol.172 , pp. 6336-6344
    • Mattioli, I.1    Sebald, A.2    Bucher, C.3    Charles, R.P.4    Nakano, H.5    Doi, T.6    Kracht, M.7    Schmitz, M.L.8
  • 33
    • 0034665748 scopus 로고    scopus 로고
    • The glucocorticoid receptor inhibits NF-κB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Nissen R.M., and Yamamoto K.R. The glucocorticoid receptor inhibits NF-κB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev. 14 (2000) 2314-2329
    • (2000) Genes Dev. , vol.14 , pp. 2314-2329
    • Nissen, R.M.1    Yamamoto, K.R.2
  • 34
    • 0037023695 scopus 로고    scopus 로고
    • Heat shock factor 1 represses transcription of the IL-1β gene through physical interaction with the nuclear factor of interleukin 6
    • Xie Y., Chen C., Stevenson M.A., Auron P.E., and Calderwood S.K. Heat shock factor 1 represses transcription of the IL-1β gene through physical interaction with the nuclear factor of interleukin 6. J. Biol. Chem. 277 (2002) 11802-11810
    • (2002) J. Biol. Chem. , vol.277 , pp. 11802-11810
    • Xie, Y.1    Chen, C.2    Stevenson, M.A.3    Auron, P.E.4    Calderwood, S.K.5
  • 35
    • 6344278116 scopus 로고    scopus 로고
    • Evidence for a role of heat shock factor 1 in inhibition of NF-κB pathway during heat shock response-mediated lung protection
    • Wirth D., Bureau F., Melotte D., Christians E., and Gustin P. Evidence for a role of heat shock factor 1 in inhibition of NF-κB pathway during heat shock response-mediated lung protection. Am. J. Physiol. Lung Cell. Mol. Physiol. 287 (2004) L953-L961
    • (2004) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.287
    • Wirth, D.1    Bureau, F.2    Melotte, D.3    Christians, E.4    Gustin, P.5
  • 36
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation
    • Zhang S.Q., Kovalenko A., Cantarella G., and Wallach D. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation. Immunity 12 (2000) 301-311
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 37
    • 0037332580 scopus 로고    scopus 로고
    • Tetrameric oligomerization of IκB kinase γ (IKKγ) is obligatory for IKK complex activity and NF-κB activation
    • Tegethoff S., Behlke J., and Scheidereit C. Tetrameric oligomerization of IκB kinase γ (IKKγ) is obligatory for IKK complex activity and NF-κB activation. Mol. Cell. Biol. 23 (2003) 2029-2041
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2029-2041
    • Tegethoff, S.1    Behlke, J.2    Scheidereit, C.3
  • 39
    • 14044256556 scopus 로고    scopus 로고
    • Detection of a novel parasite kinase activity at the Toxoplasma gondii parasitophorous vacuole membrane capable of phosphorylating host IκBα
    • Molestina R.E., and Sinai A.P. Detection of a novel parasite kinase activity at the Toxoplasma gondii parasitophorous vacuole membrane capable of phosphorylating host IκBα. Cell Microbiol. 7 (2005) 351-362
    • (2005) Cell Microbiol. , vol.7 , pp. 351-362
    • Molestina, R.E.1    Sinai, A.P.2
  • 40
    • 0036160150 scopus 로고    scopus 로고
    • Nods: a family of cytosolic proteins that regulate the host response to pathogens
    • Inohara N., Ogura Y., and Nunez G. Nods: a family of cytosolic proteins that regulate the host response to pathogens. Curr. Opin. Microbiol. 5 (2002) 76-80
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 76-80
    • Inohara, N.1    Ogura, Y.2    Nunez, G.3
  • 41
    • 23644448266 scopus 로고    scopus 로고
    • Regulation of Nod1 by Hsp90 chaperone complex
    • Hahn J.S. Regulation of Nod1 by Hsp90 chaperone complex. FEBS Lett. 579 (2005) 4513-4519
    • (2005) FEBS Lett. , vol.579 , pp. 4513-4519
    • Hahn, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.