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Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
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Citations
Cites
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491
Self-citationThe Influence of ATP and p23 on the Conformation of hsp90
Sullivan, W. P., Owen, B. A. L., & Toft, D. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207754200 · Cited by 111 · cited 1×
“…co-chaperone p23/Sba1, which only associates with Hsp90 in the ATP-bound and N-terminally dimerised form (Chadli et al, 2000; Prodromou et al, 2000; Sullivan et al, 2002), slows down the cycle by stabilising the closed conformation of the clamp, but as it binds after ATP, it cannot completely…”
Background
Research works printed but not linked: 37
- Ban C, Junop M, Yang W (1999) Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 97: 85–97 · DOI · Paper page
- Ban C, Yang W (1998) Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis. Cell 95: 541–552 · DOI · Paper page
- Beamer LJ, Carroll SF, Eisenberg D (1997) Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science 276: 1861–1864 · DOI · Paper page
- Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse‐Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D54: 905–921
- CCP4 (1994) Programs for protein crystallography. Acta Crystallogr D50: 760–763 · DOI · Paper page
- Chadli A, Bouhouche I, Sullivan W, Stensgard B, McMahon N, Catelli MG, Toft DO (2000) Dimerization and N‐terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90. Proc Natl Acad Sci USA 97: 12524–12529 · DOI
- Chen S, Smith DF (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J Biol Chem 273: 35194–35200 · DOI · Paper page
- Chen SY, Prapapanich V, Rimerman RA, Honore B, Smith DF (1996) Interactions of p60, a mediator of progesterone‐receptor assembly, with heat‐shock proteins hsp90 and hsp70. Mol Endocrinol 10: 682–693
- Chen SY, Sullivan WP, Toft DO, Smith DF (1998) Differential interactions of p23 and the TPR‐containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants. Cell Stress Chaper 3: 118–129 · DOI · Paper page
- Dolinski KJ, Cardenas ME, Heitman J (1998) CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol Cell Biol 18: 7344–7352 · DOI
- Grammatikakis N, Lin J‐H, Grammatikakis A, Tsichlis PN, Cochran BH (1999) p50cdc37 acting in concert with Hsp90 is required for Raf‐1 function. Mol Cell Biol 19: 1661–1672 · DOI · Paper page
- Jones TA, Zou J‐Y, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47: 110–119 · DOI · Paper page
- Leslie AGW (1995) MOSFLM Users Guide. Cambridge, UK: MRC Laboratory of Molecular Biology
- Lotz GP, Lin H, Harst A, Obermann WMJ (2003) 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: 17228–17235 · DOI · Paper page
- Marsh JA, Kalton HM, Gaber RF (1998) Cns1 is an essential protein associated with the Hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40‐dependent functions in cpr7delta cells. Mol Cell Biol 18: 7353–7359 · DOI
- Nathan DF, Vos MH, Lindquist S (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss‐of‐function mutation. Proc Natl Acad Sci USA 96: 1409–1414 · DOI
- Navaza J (1994) AMoRE—an automated package for molecular replacement. Acta Crystallogr D50: 157–163 · DOI · Paper page
- Obermann WMJ, Sondermann H, Russo AA, Pavletich NP, Hartl FU (1998) In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol 143: 901–910 · DOI · Paper page
- Owens‐Grillo JK, Czar MJ, Hutchinson KA, Hoffman K, Perdew GH, Pratt WB (1996a) A model of protein targetting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J Biol Chem 271: 13468–13475 · DOI · Paper page
- Owens‐Grillo JK, Hoffman K, Hutchinson KA, Yem AW, Deibel MRJ, Handschumacher RE, Pratt WB (1995) The cyclosporin A‐binding immunophilin Cyp‐40 and the FK506‐binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor. J Biol Chem 270: 20479–20484 · DOI · Paper page
- Owens‐Grillo JK, Stancato LF, Hoffmann K, Pratt WB, Krishna P (1996b) Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants. Biochemistry 35: 15249–15255 · DOI
- Panaretou B, Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH (1998) ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J 17: 4829–4836 · DOI · Paper page
- Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby‐Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C (2002) Activation of the ATPase activity of Hsp90 by the stress‐regulated co‐chaperone Aha1. Mol Cell 10: 1307–1318 · DOI · Paper page
- Pearl FMG, Lee D, Bray JE, Sillitoe I, Todd AE, Harrison AP, Thornton JM, Orengo CA (2000) Assigning genomic sequences to CATH. Nucleic Acids Res 28: 277–282 · DOI · Paper page
- Pearl LH, Prodromou C (2002) Structure, function and mechanism of the Hsp90 molecular chaperone. Adv Prot Chem 59: 157–185
- Pratt WB, Toft DO (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70‐based chaperone machinery. Exp Biol Med 228: 111–133 · DOI · Paper page
- Prodromou C, Panaretou B, Chohan S, Siligardi G, O'Brien R, Ladbury JE, Roe SM, Piper PW, Pearl LH (2000) The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains. EMBO J 19: 4383–4392 · DOI · Paper page
- Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH (1997) Identification and structural characterization of the ATP/ADP‐binding site in the Hsp90 molecular chaperone. Cell 90: 65–75 · DOI · Paper page
- Prodromou C, Siligardi G, O'Brien R, Woolfson DN, Regan L, Panaretou B, Ladbury JE, Piper PW, Pearl LH (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)‐domain co‐chaperones. EMBO J 18: 754–762 · DOI · Paper page
- Ratajczak T, Carrello A (1996) Cyclophilin‐40 (Cyp‐40), mapping of its Hsp90 binding domain and evidence that FKBP52 competes with Cyp‐40 for Hsp90 binding. J Biol Chem 271: 2961–2965 · DOI · Paper page
- Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J (2003) Sti1 is a non‐competitive inhibitor of the Hsp90 ATPase. J Biol Chem 278: 10328–10333 · DOI · Paper page
- Roussel A, Cambillau C (1991) TURBO. In Silicon Graphics Geometry Partners Directory, Vol. 81, pp 77–78. Mountain View, CA: Silicon Graphics Inc
- Sato S, Fujita N, Tsuruo T (2000) Modulation of akt kinase activity by binding to hsp90. Proc Natl Acad Sci USA 97: 10832–10837 · DOI · Paper page
- Siligardi G, Panaretou B, Meyer P, Singh S, Woolfson DN, Piper PW, Pearl LH, Prodromou C (2002) Regulation of Hsp90 ATPase activity by the co‐chaperone Cdc37p/p50cdc37. J Biol Chem 277: 20151–20159 · DOI · Paper page
- Silverstein AM, Galigniana MD, Chen M‐S, Owens‐Grillo J, Chinkers M, Pratt WB (1997) Protein phosphatase 5 is a major component of glucocorticoid receptor‐hsp90 complexes with properties of an FK506‐binding immunophilin. J Biol Chem 272: 16224–16230 · DOI · Paper page
- Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G (1991) Crystal structure of an N‐terminal fragment of the DNA gyrase B protein. Nature 351: 624–629 · DOI · Paper page
- Young JC, Hartl FU (2000) Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23. EMBO J 19: 5930–5940 · DOI · Paper page
Cited by
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103
Self-citationCrystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962
Self-citationThe Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Metadata
- Authors
- Meyer, P., Prodromou, C., Liao, C., Hu, B., Mark Roe, S., Vaughan, C. K., Vlasic, I., Panaretou, B., Piper, P. W., & Pearl, L. H.
- Venue
- The EMBO Journal
- Published
- 2004-01-22
- Volume
- 23
- Issue
- 3
- Pages
- 511-519
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W4254510769
- Cited by
- 166
- References
- 3
- FWCI
- 2.84
- Type
- journal article
- Language
- en
- Update notices
- erratum (2004-03-24)
- Open access
- green
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
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- Meyer, P., Prodromou, C., Liao, C., Hu, B., Mark Roe, S., Vaughan, C. K., Vlasic, I., Panaretou, B., Piper, P. W., & Pearl, L. H. (2004). Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. The EMBO Journal. https://doi.org/10.1038/sj.emboj.7600060
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