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Volumn 37, Issue 3, 2010, Pages 344-354

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

Author keywords

PROTEINS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; DIMER; HEAT SHOCK PROTEIN 90; PROTEIN AHA1; UNCLASSIFIED DRUG;

EID: 75949106173     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2010.01.006     Document Type: Article
Times cited : (199)

References (51)
  • 2
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., and Horwich A. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 3
    • 0141683523 scopus 로고    scopus 로고
    • NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol
    • Dehner A., Furrer J., Richter K., Schuster I., Buchner J., and Kessler H. NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol. ChemBioChem 4 (2003) 870-877
    • (2003) ChemBioChem , vol.4 , pp. 870-877
    • Dehner, A.1    Furrer, J.2    Richter, K.3    Schuster, I.4    Buchner, J.5    Kessler, H.6
  • 4
    • 34948893963 scopus 로고    scopus 로고
    • Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
    • Dollins D.E., Warren J.J., Immormino R.M., and Gewirth D.T. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol. Cell 28 (2007) 41-56
    • (2007) Mol. Cell , vol.28 , pp. 41-56
    • Dollins, D.E.1    Warren, J.J.2    Immormino, R.M.3    Gewirth, D.T.4
  • 5
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan C.Y., Lee S., and Cyr D.M. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8 (2003) 309-316
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 6
    • 43249105354 scopus 로고    scopus 로고
    • p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
    • Forafonov F., Toogun O.A., Grad I., Suslova E., Freeman B.C., and Picard D. p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol. Cell. Biol. 28 (2008) 3446-3456
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3446-3456
    • Forafonov, F.1    Toogun, O.A.2    Grad, I.3    Suslova, E.4    Freeman, B.C.5    Picard, D.6
  • 7
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • Geller R., Vignuzzi M., Andino R., and Frydman J. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 21 (2007) 195-205
    • (2007) Genes Dev. , vol.21 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 9
    • 62049084010 scopus 로고    scopus 로고
    • Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
    • Graf C., Stankiewicz M., Kramer G., and Mayer M.P. Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J. 28 (2009) 602-613
    • (2009) EMBO J. , vol.28 , pp. 602-613
    • Graf, C.1    Stankiewicz, M.2    Kramer, G.3    Mayer, M.P.4
  • 10
    • 18844406200 scopus 로고    scopus 로고
    • Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation
    • Harst A., Lin H., and Obermann W.M. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem. J. 387 (2005) 789-796
    • (2005) Biochem. J. , vol.387 , pp. 789-796
    • Harst, A.1    Lin, H.2    Obermann, W.M.3
  • 11
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle P., Siepmann M., Harst A., Siderius M., Reusch H.P., and Obermann W.M. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell. Biol. 26 (2006) 8385-8395
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, H.P.5    Obermann, W.M.6
  • 12
    • 61949349758 scopus 로고    scopus 로고
    • Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
    • Hessling M., Richter K., and Buchner J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 16 (2009) 287-293
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 287-293
    • Hessling, M.1    Richter, K.2    Buchner, J.3
  • 13
    • 40449089789 scopus 로고    scopus 로고
    • Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin
    • Holmes J.L., Sharp S.Y., Hobbs S., and Workman P. Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Cancer Res. 68 (2008) 1188-1197
    • (2008) Cancer Res. , vol.68 , pp. 1188-1197
    • Holmes, J.L.1    Sharp, S.Y.2    Hobbs, S.3    Workman, P.4
  • 14
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • Johnson J.L., Beito T.G., Krco C.J., and Toft D.O. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14 (1994) 1956-1963
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Krco, C.J.3    Toft, D.O.4
  • 15
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • Johnson J., Corbisier R., Stensgard B., and Toft D. The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 56 1-6 Spec No (1996) 31-37
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.56 , Issue.1-6 Spec No , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.4
  • 16
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates Hsp70/Hsp90 interactions in protein folding
    • Johnson B.D., Schumacher R.J., Ross E.D., and Toft D.O. Hop modulates Hsp70/Hsp90 interactions in protein folding. J. Biol. Chem. 273 (1998) 3679-3686
    • (1998) J. Biol. Chem. , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 17
    • 0037593900 scopus 로고    scopus 로고
    • Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
    • Lotz G.P., Lin H., Harst A., and Obermann W.M. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. 278 (2003) 17228-17235
    • (2003) J. Biol. Chem. , vol.278 , pp. 17228-17235
    • Lotz, G.P.1    Lin, H.2    Harst, A.3    Obermann, W.M.4
  • 19
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • McClellan A.J., Xia Y., Deutschbauer A.M., Davis R.W., Gerstein M., and Frydman J. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131 (2007) 121-135
    • (2007) Cell , vol.131 , pp. 121-135
    • McClellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5    Frydman, J.6
  • 22
    • 61949212626 scopus 로고    scopus 로고
    • The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
    • Mickler M., Hessling M., Ratzke C., Buchner J., and Hugel T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat. Struct. Mol. Biol. 16 (2009) 281-286
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 281-286
    • Mickler, M.1    Hessling, M.2    Ratzke, C.3    Buchner, J.4    Hugel, T.5
  • 23
    • 0033574059 scopus 로고    scopus 로고
    • Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation
    • Nathan D.F., Vos M.H., and Lindquist S. Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc. Natl. Acad. Sci. USA 96 (1999) 1409-1414
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1409-1414
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 24
    • 61949212454 scopus 로고    scopus 로고
    • Visualizing the twists and turns of a molecular chaperone
    • Neckers L., Tsutsumi S., and Mollapour M. Visualizing the twists and turns of a molecular chaperone. Nat. Struct. Mol. Biol. 16 (2009) 235-236
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 235-236
    • Neckers, L.1    Tsutsumi, S.2    Mollapour, M.3
  • 26
    • 44349097402 scopus 로고    scopus 로고
    • Structural studies on the co-chaperone Hop and its complexes with Hsp90
    • Onuoha S.C., Coulstock E.T., Grossmann J.G., and Jackson S.E. Structural studies on the co-chaperone Hop and its complexes with Hsp90. J. Mol. Biol. 379 (2008) 732-744
    • (2008) J. Mol. Biol. , vol.379 , pp. 732-744
    • Onuoha, S.C.1    Coulstock, E.T.2    Grossmann, J.G.3    Jackson, S.E.4
  • 27
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., and Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17 (1998) 4829-4836
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 30
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 59 (2002) 1640-1648
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 31
    • 0034968225 scopus 로고    scopus 로고
    • Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
    • Pirkl F., and Buchner J. Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J. Mol. Biol. 308 (2001) 795-806
    • (2001) J. Mol. Biol. , vol.308 , pp. 795-806
    • Pirkl, F.1    Buchner, J.2
  • 32
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt W.B., and Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228 (2003) 111-133
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 33
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of Hsp90
    • Prodromou C., and Pearl L.H. Structure and functional relationships of Hsp90. Curr. Cancer Drug Targets 3 (2003) 301-323
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 35
  • 36
    • 0346037322 scopus 로고    scopus 로고
    • N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle
    • Richter K., Reinstein J., and Buchner J. N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J. Biol. Chem. 277 (2002) 44905-44910
    • (2002) J. Biol. Chem. , vol.277 , pp. 44905-44910
    • Richter, K.1    Reinstein, J.2    Buchner, J.3
  • 37
    • 0037518202 scopus 로고    scopus 로고
    • Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle
    • Richter K., Muschler P., Hainzl O., Reinstein J., and Buchner J. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J. Biol. Chem. 278 (2003) 10328-10333
    • (2003) J. Biol. Chem. , vol.278 , pp. 10328-10333
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Reinstein, J.4    Buchner, J.5
  • 38
    • 4444291743 scopus 로고    scopus 로고
    • The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • Richter K., Walter S., and Buchner J. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 342 (2004) 1403-1413
    • (2004) J. Mol. Biol. , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3
  • 41
    • 0036700126 scopus 로고    scopus 로고
    • Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone
    • Salek R.M., Williams M.A., Prodromou C., Pearl L.H., and Ladbury J.E. Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone. J. Biomol. NMR 23 (2002) 327-328
    • (2002) J. Biomol. NMR , vol.23 , pp. 327-328
    • Salek, R.M.1    Williams, M.A.2    Prodromou, C.3    Pearl, L.H.4    Ladbury, J.E.5
  • 42
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 43
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
    • Scheibel T., Weikl T., and Buchner J. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. USA 95 (1998) 1495-1499
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1495-1499
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 44
    • 33750008686 scopus 로고    scopus 로고
    • Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • Shiau A.K., Harris S.F., Southworth D.R., and Agard D.A. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 127 (2006) 329-340
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 45
  • 47
    • 0037195951 scopus 로고    scopus 로고
    • The influence of ATP and p23 on the conformation of hsp90
    • Sullivan W.P., Owen B.A., and Toft D.O. The influence of ATP and p23 on the conformation of hsp90. J. Biol. Chem. 277 (2002) 45942-45948
    • (2002) J. Biol. Chem. , vol.277 , pp. 45942-45948
    • Sullivan, W.P.1    Owen, B.A.2    Toft, D.O.3
  • 49
    • 31444454302 scopus 로고    scopus 로고
    • The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
    • Wandinger S.K., Suhre M.H., Wegele H., and Buchner J. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. 25 (2006) 367-376
    • (2006) EMBO J. , vol.25 , pp. 367-376
    • Wandinger, S.K.1    Suhre, M.H.2    Wegele, H.3    Buchner, J.4
  • 51
    • 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., and Neckers L. Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nat. Struct. Mol. Biol. 12 (2005) 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


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