메뉴 건너뛰기




Volumn 31, Issue 12, 2012, Pages 1582-1591

Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1

Author keywords

chaperones; CHIP; Hsp90; LKB1; tumor suppressor

Indexed keywords

CELL CYCLE PROTEIN 37; CHAPERONE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 90; MULTIPROTEIN COMPLEX; PROTEIN; PROTEIN KINASE LKB1; PROTEIN STRAD; RECOMBINANT PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84860407614     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2011.342     Document Type: Article
Times cited : (42)

References (46)
  • 3
    • 1542777034 scopus 로고    scopus 로고
    • Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD
    • DOI 10.1016/S0092-8674(04)00114-X, PII S009286740400114X
    • Baas AF, Kuipers J, van der Wel NN, Batlle E, Koerten HK, Peters PJ et al. (2004). Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD. Cell 116: 457-466. (Pubitemid 38366321)
    • (2004) Cell , vol.116 , Issue.3 , pp. 457-466
    • Baas, A.F.1    Kuipers, J.2    Van Der Wel, N.N.3    Batlle, E.4    Koerten, H.K.5    Peters, P.J.6    Clevers, H.C.7
  • 4
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger CA, Connell P, Wu Y, Thompson LJ, Yin LY, Patterson C. (1999). Identification of CHIP, a novel tetratricopeptide repeatcontaining protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 19: 4535-4545. (Pubitemid 29242026)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.-Y.6    Patterson, C.7
  • 5
    • 33750478283 scopus 로고    scopus 로고
    • Depletion of the co-chaperone CDC-37 reveals two modes of PAR-6 cortical association in C. elegans embryos
    • DOI 10.1242/dev.02544
    • Beers M, Kemphues K. (2006). Depletion of the co-chaperone CDC-37 reveals two modes of PAR-6 cortical association in C. elegans embryos. Development 133: 3745-3754. (Pubitemid 44650953)
    • (2006) Development , vol.133 , Issue.19 , pp. 3745-3754
    • Beers, M.1    Kemphues, K.2
  • 7
    • 0037444766 scopus 로고    scopus 로고
    • Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability
    • DOI 10.1042/BJ20021813
    • Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR. (2003a). Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability. Biochem J 370: 849-857. (Pubitemid 36399076)
    • (2003) Biochemical Journal , vol.370 , Issue.3 , pp. 849-857
    • Boudeau, J.1    Deak, M.2    Lawlor, M.A.3    Morrice, N.A.4    Alessi, D.R.5
  • 8
    • 1842581909 scopus 로고    scopus 로고
    • Comprehensive Proteomic Analysis of Human Par Protein Complexes Reveals an Interconnected Protein Network
    • DOI 10.1074/jbc.M312171200
    • Brajenovic M, Joberty G, Küster B, Bouwmeester T, Drewes G. (2004). Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. J Biol Chem 279: 12804-12811. (Pubitemid 38445853)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12804-12811
    • Brajenovic, M.1    Joberty, G.2    Kuster, B.3    Bouwmeester, T.4    Drewes, G.5
  • 9
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Review
    • Caplan AJ, Mandal AK, Theodoraki MA. (2007). Molecular chaperones and protein kinase quality control. Trends Cell Biol 17: 87-92. Review.
    • (2007) Trends Cell Biol , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 12
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1: Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • DOI 10.1101/gad.1199104
    • Corradetti MN, Inoki K, Bardeesy N, DePinho RA, Guan KL. (2004). Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev 18: 1533-1538. (Pubitemid 38868905)
    • (2004) Genes and Development , vol.18 , Issue.13 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    DePinho, R.A.4    Guan, K.-L.5
  • 13
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • DOI 10.1016/S0968-0004(02)02125-4, PII S0968000402021254
    • Cyr DM, Höhfeld J, Patterson C. (2002). Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem Sci 27: 368-375. (Pubitemid 34756520)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.7 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 14
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • DOI 10.1016/S0960-9822(01)00487-0
    • Demand J, Alberti S, Patterson C, Höhfeld J. (2001). Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol 11: 1569-1577. (Pubitemid 32978521)
    • (2001) Current Biology , vol.11 , Issue.20 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 15
    • 58649094677 scopus 로고    scopus 로고
    • Characterization of an alternative splice variant of LKB1
    • Denison FC, Hiscock NJ, Carling D,Woods A. (2009). Characterization of an alternative splice variant of LKB1. J Biol Chem 284: 67-76.
    • (2009) J Biol Chem , vol.284 , pp. 67-76
    • Denison, F.C.1    Hiscock, N.J.2    Carling, D.3    Woods, A.4
  • 16
    • 0035898534 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR
    • DOI 10.1093/emboj/20.14.3771
    • Donzé O, Abbas-Terki T, Picard D. (2001). The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNAdependent kinase PKR. EMBO J 20: 3771-3780. (Pubitemid 32691788)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3771-3780
    • Donze, O.1    Abbas-Terki, T.2    Picard, D.3
  • 18
    • 28144439277 scopus 로고    scopus 로고
    • CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-α
    • DOI 10.1210/me.2005-0111
    • Fan M, Park A, Nephew KP. (2005). CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycininduced degradation of estrogen receptor-alpha. Mol Endocrinol 19: 2901-2914. (Pubitemid 41697710)
    • (2005) Molecular Endocrinology , vol.19 , Issue.12 , pp. 2901-2914
    • Fan, M.1    Park, A.2    Nephew, K.P.3
  • 19
    • 37349041710 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease
    • Review
    • Hardie DG. (2008). Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease. FEBS Lett 582: 81-89. Review.
    • (2008) FEBS Lett , vol.582 , pp. 81-89
    • Hardie, D.G.1
  • 20
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley SA, Boudeau J, Reid JL, Mustard KJ, Udd L, MäkeläTP et al. (2003). Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J Biol 2: 28.
    • (2003) J Biol , vol.2 , pp. 28
    • Hawley, S.A.1    Boudeau, J.2    Reid, J.L.3    Mustard, K.J.4    Udd, L.5    Mäkelätp6
  • 22
    • 56749176442 scopus 로고    scopus 로고
    • LKB1; Linking cell structure and tumor suppression
    • Review
    • Hezel AF, Bardeesy N. (2008). LKB1; linking cell structure and tumor suppression. Oncogene 27: 6908-6919. Review.
    • (2008) Oncogene , vol.27 , pp. 6908-6919
    • Hezel, A.F.1    Bardeesy, N.2
  • 24
    • 67650898228 scopus 로고    scopus 로고
    • LKB1 and AMPK family signaling: The intimate link between cell polarity and energy metabolism
    • Review
    • Jansen M, Ten Klooster JP, Offerhaus GJ, Clevers H. (2009). LKB1 and AMPK family signaling: the intimate link between cell polarity and energy metabolism. Physiol Rev 89: 777-798. Review.
    • (2009) Physiol Rev , vol.89 , pp. 777-798
    • Jansen, M.1    Ten Klooster, J.P.2    Offerhaus, G.J.3    Clevers, H.4
  • 29
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • Review
    • McDonough H, Patterson C. (2003). CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8: 303-308. Review.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 30
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • DOI 10.1038/35050509
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. (2001). The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3: 100-105. (Pubitemid 32114840)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 31
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • Review
    • Murata S, Chiba T, Tanaka K. (2003). CHIP: a quality-control E3 ligase collaborating with molecular chaperones. Int J Biochem Cell Biol 35: 572-578. Review.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 32
    • 0346057795 scopus 로고    scopus 로고
    • Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37
    • DOI 10.1038/sj.onc.1207179
    • Nony P, Gaude H, Rossel M, Fournier L, Rouault JP, Billaud M. (2003). Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37. Oncogene 22: 9165-9175. (Pubitemid 38067992)
    • (2003) Oncogene , vol.22 , Issue.57 , pp. 9165-9175
    • Nony, P.1    Gaude, H.2    Rossel, M.3    Fournier, L.4    Rouault, J.-P.5    Billaud, M.6
  • 34
    • 70349921403 scopus 로고    scopus 로고
    • Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol
    • Sreeramulu S, Gande SL, Göbel M, Schwalbe H. (2009). Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol. Angew Chem Int Ed Engl 48: 5853-5855.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 5853-5855
    • Sreeramulu, S.1    Gande, S.L.2    Göbel, M.3    Schwalbe, H.4
  • 35
    • 0031054517 scopus 로고    scopus 로고
    • The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
    • DOI 10.1074/jbc.272.7.4013
    • Stancato LF, Silverstein AM, Owens-Grillo JK, Chow YH, Jove R, Pratt WB. (1997). The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem 272: 4013-4020. (Pubitemid 27078462)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 4013-4020
    • Stancato, L.F.1    Silverstein, A.M.2    Owens-Grillo, J.K.3    Chow, Y.-H.4    Jove, R.5    Pratt, W.B.6
  • 36
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova L, Leng X, Parker SB, Harper JW. (1996). Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 10: 1491-1502. (Pubitemid 26260706)
    • (1996) Genes and Development , vol.10 , Issue.12 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Wade Harper, J.4
  • 37
    • 56049117647 scopus 로고    scopus 로고
    • A novel short splice variant of the tumour suppressor LKB1 is required for spermiogenesis
    • Towler MC, Fogarty S, Hawley SA, Pan DA, Martin DM, Morrice NA et al. (2008). A novel short splice variant of the tumour suppressor LKB1 is required for spermiogenesis. Biochem J 416: 1-14.
    • (2008) Biochem J , vol.416 , pp. 1-14
    • Towler, M.C.1    Fogarty, S.2    Hawley, S.A.3    Pan, D.A.4    Martin, D.M.5    Morrice, N.A.6
  • 38
    • 52249108496 scopus 로고    scopus 로고
    • Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37
    • Vaughan CK, Mollapour M, Smith JR, Truman A, Hu B, Good VM et al. (2008). Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol Cell 31: 886-895.
    • (2008) Mol Cell , vol.31 , pp. 886-895
    • Vaughan, C.K.1    Mollapour, M.2    Smith, J.R.3    Truman, A.4    Hu, B.5    Good, V.M.6
  • 39
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • DOI 10.1038/nrc1716
    • Whitesell L, Lindquist SL. (2005). Hsp90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772. Review. (Pubitemid 41400776)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 41
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu W, Marcu M, Yuan X, Mimnaugh E, Patterson C, Neckers L. (2002). Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc Natl Acad Sci USA 99: 12847-12852.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 42
    • 33845804718 scopus 로고    scopus 로고
    • Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity
    • DOI 10.1128/MCB.00899-06
    • Xu W, Yuan X, Beebe K, Xiang Z, Neckers L. (2007). Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity. Mol Cell Biol 27: 220-228. (Pubitemid 46013246)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.1 , pp. 220-228
    • Xu, W.1    Yuan, X.2    Beebe, K.3    Xiang, Z.4    Neckers, L.5
  • 43
    • 15544372341 scopus 로고    scopus 로고
    • Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex
    • Xu W, Yuan X, Xiang Z, Mimnaugh E, Marcu M, Neckers L. (2005). Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nat Struct Mol Biol 12: 120-126.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 120-126
    • Xu, W.1    Yuan, X.2    Xiang, Z.3    Mimnaugh, E.4    Marcu, M.5    Neckers, L.6
  • 44
    • 55749096409 scopus 로고    scopus 로고
    • Inhibition of Hsp90 activates osteoclast c-Src signaling and promotes growth of prostate carcinoma cells in bone
    • Yano A, Tsutsumi S, Soga S, Lee MJ, Trepel J, Osada H et al. (2008). Inhibition of Hsp90 activates osteoclast c-Src signaling and promotes growth of prostate carcinoma cells in bone. Proc Natl Acad Sci USA 105: 15541-15546.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15541-15546
    • Yano, A.1    Tsutsumi, S.2    Soga, S.3    Lee, M.J.4    Trepel, J.5    Osada, H.6
  • 45
    • 72949115493 scopus 로고    scopus 로고
    • Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation
    • Zeqiraj E, Filippi BM, Deak M, Alessi DR, van Aalten DM. (2009). Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation. Science 326: 1707-1711.
    • (2009) Science , vol.326 , pp. 1707-1711
    • Zeqiraj, E.1    Filippi, B.M.2    Deak, M.3    Alessi, D.R.4    Van Aalten, D.M.5
  • 46
    • 72149125851 scopus 로고    scopus 로고
    • Characterization of celastrol to inhibit Hsp90 and Cdc37 interaction
    • Zhang T, Li Y, Yu Y, Zou P, Jiang Y, Sun D. (2009). Characterization of celastrol to inhibit Hsp90 and Cdc37 interaction. J Biol Chem 284: 35381-35389.
    • (2009) J Biol Chem , vol.284 , pp. 35381-35389
    • Zhang, T.1    Li, Y.2    Yu, Y.3    Zou, P.4    Jiang, Y.5    Sun, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.