Overexpression of the Cochaperone CHIP Enhances Hsp70-Dependent Folding Activity in Mammalian Cells

REFERENCES

• Aravind, L., and E. V. Koonin. 2000. The U box is a modified RING finger — a common domain in ubiquitination. Curr. Biol. 10: R132–R134.
   PubMed Web of Science ®Google Scholar
• Ballinger, C. A., P. Connell, Y. Wu, Z. Hu, L. J. Thompson, L. Y. Yin, and C. Patterson. 1999. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19: 4535–4545.
   PubMed Web of Science ®Google Scholar
• Beckmann, R. P., L. A. Mizzen, and W. J. Welch. 1990. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248: 850–854.
   PubMed Web of Science ®Google Scholar
• Bimston, D., J. H. Song, D. Winchester, S. Takayama, J. C. Reed, and R. I. Morimoto. 1998. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J. 17: 6871–6878.
   PubMed Web of Science ®Google Scholar
• Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351–366.
   PubMed Web of Science ®Google Scholar
• Cheetham, M. E., A. P. Jackson, and B. H. Anderton. 1994. Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Eur. J. Biochem. 226: 99–107.
   PubMedGoogle Scholar
• Connell, P., C. A. Ballinger, J. Jiang, Y. Wu, L. J. Thompson, J. Hohfeld, and C. Patterson. 2001. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell. Biol. 3: 93–96.
   PubMed Web of Science ®Google Scholar
• Demand, J., S. Alberti, C. Patterson, and J. Hohfeld. 2001. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11: 1569–1577.
   PubMed Web of Science ®Google Scholar
• Flynn, G. C., T. G. Chappell, and J. E. Rothman. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245: 385–390.
   PubMed Web of Science ®Google Scholar
• Gebauer, M., M. Zeiner, and U. Gehring. 1997. Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 417: 109–113.
   PubMedGoogle Scholar
• Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381: 571–580.
   PubMed Web of Science ®Google Scholar
• Hohfeld, J., Y. Minami, and F. U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589–598.
   PubMed Web of Science ®Google Scholar
• Jiang, J., C. A. Ballinger, Y. Wu, Q. Dai, D. M. Cyr, J. Hohfeld, and C. Patterson. 2001. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276: 42938–42944.
   PubMed Web of Science ®Google Scholar
• Kabakov, A. E., K. R. Budagova, D. S. Latchman, and H. H. Kampinga. 2002. Stressful preconditioning and HSP70 overexpression attenuate proteotoxicity of cellular ATP depletion. Am. J. Physiol. 283: C521–C534.
   Google Scholar
• Koegl, M., T. Hoppe, S. Schlenker, H. D. Ulrich, T. U. Mayer, and S. Jentsch. 1999. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96: 635–644.
   PubMed Web of Science ®Google Scholar
• Laufen, T., M. P. Mayer, C. Beisel, D. Klostermeier, A. Mogk, J. Reinstein, and B. Bukau. 1999. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc. Natl. Acad. Sci. USA 96: 5452–5457.
   PubMed Web of Science ®Google Scholar
• Lee, S., C. Y. Fan, J. M. Younger, H. Ren, and D. M. Cyr. 2002. Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding. J. Biol. Chem. 277: 21675–21682.
   PubMedGoogle Scholar
• Loktionova, S. A., O. P. Ilyinskaya, and A. E. Kabakov. 1998. Early and delayed tolerance to simulated ischemia in heat-preconditioned endothelial cells: a role for HSP27. Am. J. Physiol. 275: H2147–H2158.
   PubMedGoogle Scholar
• Luders, J., J. Demand, S. Schonfelder, M. Frien, R. Zimmermann, and J. Hohfeld. 1998. Cofactor-induced modulation of the functional specificity of the molecular chaperone Hsc70. Biol. Chem. 379: 1217–1226.
   PubMedGoogle Scholar
• Mayer, M. P., H. Schroder, S. Rudiger, K. Paal, T. Laufen, and B. Bukau. 2000. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7: 586–593.
   PubMedGoogle Scholar
• Meacham, G. C., C. Patterson, W. Zhang, J. M. Younger, and D. M. Cyr. 2001. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell. Biol. 3: 100–105.
   PubMed Web of Science ®Google Scholar
• Michels, A. A., B. Kanon, O. Bensaude, and H. H. Kampinga. 1999. Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells. J. Biol. Chem. 274: 36757–36763.
   PubMedGoogle Scholar
• Michels, A. A., B. Kanon, A. W. T. Konings, K. Ohtsuka, O. Bensaude, and H. H. Kampinga. 1997. Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem. 272: 33283–33289.
   PubMed Web of Science ®Google Scholar
• Michels, A. A., V. T. Nguyen, A. W. Konings, H. H. Kampinga, and O. Bensaude. 1995. Thermostability of a nuclear-targeted luciferase expressed in mammalian cells. Destabilizing influence of the intranuclear microenvironment. Eur. J. Biochem. 234: 382–389.
   PubMedGoogle Scholar
• Minami, Y., J. Hohfeld, K. Ohtsuka, and F. U. Hartl. 1996. Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. J. Biol. Chem. 271: 19617–19624.
   PubMed Web of Science ®Google Scholar
• Morimoto, R. I. 1998. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12: 3788–3796.
   PubMed Web of Science ®Google Scholar
• Murata, S., Y. Minami, M. Minami, T. Chiba, and K. Tanaka. 2001. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2: 1133–1138.
   PubMed Web of Science ®Google Scholar
• Nollen, E. A., J. F. Brunsting, H. Roelofsen, L. A. Weber, and H. H. Kampinga. 1999. In vivo chaperone activity of heat shock protein 70 and thermotolerance. Mol. Cell. Biol. 19: 2069–2079.
   PubMed Web of Science ®Google Scholar
• Nollen, E. A., J. F. Brunsting, J. Song, H. H. Kampinga, and R. I. Morimoto. 2000. Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity. Mol. Cell. Biol. 20: 1083–1088.
   PubMed Web of Science ®Google Scholar
• Nollen, E. A., A. E. Kabakov, J. F. Brunsting, B. Kanon, J. Hohfeld, and H. H. Kampinga. 2001. Modulation of in vivo HSP70 chaperone activity by Hip and Bag-1. J. Biol. Chem. 276: 4677–4682.
   PubMed Web of Science ®Google Scholar
• Obermann, W. M. J., H. Sondermann, A. A. Russo, N. P. Pavletich, and F. U. Hartl. 1998. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143: 901–910.
   PubMed Web of Science ®Google Scholar
• Rudiger, S., A. Buchberger, and B. Bukau. 1997. Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4: 342–349.
   PubMedGoogle Scholar
• Schmid, D., A. Baici, H. Gehring, and P. Christen. 1994. Kinetics of molecular chaperone action. Science 263: 971–973.
   PubMed Web of Science ®Google Scholar
• Schneider, C., L. SeppLorenzino, E. Nimmesgern, O. Ouerfelli, S. Danishefsky, N. Rosen, and F. U. Hartl. 1996. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. USA 93: 14536–14541.
   PubMed Web of Science ®Google Scholar
• Sondermann, H., C. Scheufler, C. Schneider, J. Hohfeld, F. U. Hartl, and I. Moarefi. 2001. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291: 1553–1557.
   PubMed Web of Science ®Google Scholar
• Takayama, S., D. N. Bimston, S. Matsuzawa, B. C. Freeman, C. Aimesempe, Z. H. Xie, R. I. Morimoto, and J. C. Reed. 1997. BAG-1 modulates the chaperone activity of Hsp70/Hsc70. EMBO J. 16: 4887–4896.
   PubMed Web of Science ®Google Scholar
• Wall, D., M. Zylicz, and C. Georgopoulos. 1995. The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J. Biol. Chem. 270: 2139–2144.
   PubMedGoogle Scholar
• Wickner, S., M. R. Maurizi, and S. Gottesman. 1999. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888–1893.
   PubMed Web of Science ®Google Scholar