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Volumn 9, Issue 12, 2008, Pages 1193-1195

A stress protein interface of innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90; ISOPROTEIN; MUTANT PROTEIN; NUCLEOTIDE; PROTEASOME;

EID: 57049175015     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2008.208     Document Type: Article
Times cited : (6)

References (39)
  • 4
    • 20444426395 scopus 로고    scopus 로고
    • RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance
    • Bieri S et al (2004) RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance. Plant Cell 16: 3480-3495
    • (2004) Plant Cell , vol.16 , pp. 3480-3495
    • Bieri, S.1
  • 5
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose S, Weikl T, Bügl H, Buchner J (1996) Chaperone function of Hsp90-associated proteins. Science 274: 1715-1717
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bügl, H.3    Buchner, J.4
  • 6
    • 37849007364 scopus 로고    scopus 로고
    • Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity
    • Botör M et al (2007) Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity. Plant Cell 19 3791-3804
    • (2007) Plant Cell , vol.19 , pp. 3791-3804
    • Botör, M.1
  • 8
    • 33845959149 scopus 로고    scopus 로고
    • Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p
    • Catlett MG, Kaplan KB (2006) Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J Biol Chem 281: 33739-33748
    • (2006) J Biol Chem , vol.281 , pp. 33739-33748
    • Catlett, M.G.1    Kaplan, K.B.2
  • 9
    • 33746588172 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex regulates GDI-dependent Rab recycling
    • Chen CY, Balch WE (2006) The Hsp90 chaperone complex regulates GDI-dependent Rab recycling. Mol Biol Cell 17: 3494-3507
    • (2006) Mol Biol Cell , vol.17 , pp. 3494-3507
    • Chen, C.Y.1    Balch, W.E.2
  • 12
    • 0036692080 scopus 로고    scopus 로고
    • Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast
    • Dubacq C, Guerois R, Courbeyrette R, Kitagawa K, Mann C (2002) Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast. Eukaryot Cell 1: 568-582
    • (2002) Eukaryot Cell , vol.1 , pp. 568-582
    • Dubacq, C.1    Guerois, R.2    Courbeyrette, R.3    Kitagawa, K.4    Mann, C.5
  • 13
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman BC, Toft DO, Morimoto RI (1996) Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274: 1718-1720
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 14
    • 0037048699 scopus 로고    scopus 로고
    • p23 and HSP20/ alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families
    • Garcia-Ranea J, Mirey G, Camonis J, Valencia A (2002) p23 and HSP20/ alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families. FEBS Lett 529: 162-167
    • (2002) FEBS Lett , vol.529 , pp. 162-167
    • Garcia-Ranea, J.1    Mirey, G.2    Camonis, J.3    Valencia, A.4
  • 15
    • 35549009435 scopus 로고    scopus 로고
    • Involvement of the 90-kDa heat shock protein (Hsp-90) in CB2 cannabinoid receptor-mediated cell migration: A new role of Hsp-90 in migration signaling of a G protein-coupled receptor
    • He F, Qiao ZH, Cai J, Pierce W, He DC, Song ZH (2007) Involvement of the 90-kDa heat shock protein (Hsp-90) in CB2 cannabinoid receptor-mediated cell migration: A new role of Hsp-90 in migration signaling of a G protein-coupled receptor. Mol Pharmacol 72: 1289-1300
    • (2007) Mol Pharmacol , vol.72 , pp. 1289-1300
    • He, F.1    Qiao, Z.H.2    Cai, J.3    Pierce, W.4    He, D.C.5    Song, Z.H.6
  • 17
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones JD, Dangl JL (2006) The plant immune system. Nature 444 323-329
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 18
    • 57049133465 scopus 로고    scopus 로고
    • Structural and functional analysis of SGT1-HSP90 core complex required for innate immunity in plants
    • Kadota Y, Amigues B, Ducassou L, Madaoui H, Ochsenbein F, Guerois R, Shirasu K (2008) Structural and functional analysis of SGT1-HSP90 core complex required for innate immunity in plants. EMBO Rep 9: 1209-1215
    • (2008) EMBO Rep , vol.9 , pp. 1209-1215
    • Kadota, Y.1    Amigues, B.2    Ducassou, L.3    Madaoui, H.4    Ochsenbein, F.5    Guerois, R.6    Shirasu, K.7
  • 20
    • 0033166694 scopus 로고    scopus 로고
    • SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex
    • Kitagawa K, Skowyra D, Elledge SJ, Harper JW, Hieter P (1999) SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Mol Cell 4: 21-33
    • (1999) Mol Cell , vol.4 , pp. 21-33
    • Kitagawa, K.1    Skowyra, D.2    Elledge, S.J.3    Harper, J.W.4    Hieter, P.5
  • 21
    • 42949147146 scopus 로고    scopus 로고
    • Multiple conformations of E. coli Hsp90 in solution: Insights into the conformational dynamics of Hsp90
    • Krukenberg KA, Forster F, Rice LM, Sali A, Agard DA (2008) Multiple conformations of E. coli Hsp90 in solution: Insights into the conformational dynamics of Hsp90. Structure 16: 755-765
    • (2008) Structure , vol.16 , pp. 755-765
    • Krukenberg, K.A.1    Forster, F.2    Rice, L.M.3    Sali, A.4    Agard, D.A.5
  • 22
    • 0021708673 scopus 로고
    • Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies
    • Lai B-T, Chin NW, Stanek AE, Keh W, Lanks KW (1984) Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies. Mol Cell Biol 4: 2802-2810
    • (1984) Mol Cell Biol , vol.4 , pp. 2802-2810
    • Lai, B.-T.1    Chin, N.W.2    Stanek, A.E.3    Keh, W.4    Lanks, K.W.5
  • 23
    • 1942436961 scopus 로고    scopus 로고
    • Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain
    • Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ (2004) Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. J Biol Chem 279: 16511-16517
    • (2004) J Biol Chem , vol.279 , pp. 16511-16517
    • Lee, Y.T.1    Jacob, J.2    Michowski, W.3    Nowotny, M.4    Kuznicki, J.5    Chazin, W.J.6
  • 24
    • 34247265509 scopus 로고    scopus 로고
    • A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses
    • Mayor A, Martinon F, De Smedt T, Petrilli V, Tschopp J (2007) A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol 8: 497-503
    • (2007) Nat Immunol , vol.8 , pp. 497-503
    • Mayor, A.1    Martinon, F.2    De Smedt, T.3    Petrilli, V.4    Tschopp, J.5
  • 25
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan AJ, Scott MD, Frydman J (2005) Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 121: 739-748
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 26
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human Hsp90 by a client protein
    • McLaughlin SH, Smith HW, Jackson SE (2002) Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J Mol Biol 315: 787-798
    • (2002) J Mol Biol , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 27
    • 34248187981 scopus 로고    scopus 로고
    • Heat shock protein 90: The cancer chaperone
    • Neckers L (2007) Heat shock protein 90: The cancer chaperone. J Biosci 32: 517-530
    • (2007) J Biosci , vol.32 , pp. 517-530
    • Neckers, L.1
  • 28
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATpase activity of Hsp90 by the stress-regulated cochaperone Aha1
    • Panaretou B et al (2002) Activation of the ATpase activity of Hsp90 by the stress-regulated cochaperone Aha1. Mol Cell 10: 1307-1318
    • (2002) Mol Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 29
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C (2006) Structure and mechanism of the hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271-294
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 30
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl LH, Prodromou C, Workman P (2008) The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J 410: 439-453
    • (2008) Biochem J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 31
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D (2002) Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 59: 1640-1648
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 34
    • 0032724487 scopus 로고    scopus 로고
    • A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans
    • Shirasu K, Lahaye T, Tan MW, Zhou F, Azevedo C, Schulze-Lefert P (1999) A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. Cell 99: 355-366
    • (1999) Cell , vol.99 , pp. 355-366
    • Shirasu, K.1    Lahaye, T.2    Tan, M.W.3    Zhou, F.4    Azevedo, C.5    Schulze-Lefert, P.6
  • 36
    • 0141705339 scopus 로고    scopus 로고
    • HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis
    • Takahashi A, Casais C, Ichimura K, Shirasu K (2003) HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc Natl Acad Sci USA 100: 11777-11782
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11777-11782
    • Takahashi, A.1    Casais, C.2    Ichimura, K.3    Shirasu, K.4
  • 38
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.