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Science 3 December 1999:
Vol. 286. no. 5446, pp. 1888 - 1893
DOI: 10.1126/science.286.5446.1888
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Review

Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins

Sue Wickner, 1 Michael R. Maurizi, 2 Susan Gottesman 1*

Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over protein structure and function depends on molecular chaperones and proteases, both of which can recognize hydrophobic regions exposed on unfolded polypeptides. Molecular chaperones promote proper protein folding and prevent aggregation, and energy-dependent proteases eliminate irreversibly damaged proteins. The kinetics of partitioning between chaperones and proteases determines whether a protein will be destroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloid diseases.

1 Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA.
2 Laboratory of Cell Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA.
*   To whom correspondence should be addressed: E-mail: susang{at}helix.nih.gov

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Chaperone-dependent Regulation of Endothelial Nitric-oxide Synthase Intracellular Trafficking by the Co-chaperone/Ubiquitin Ligase CHIP.
J. Jiang, D. Cyr, R. W. Babbitt, W. C. Sessa, and C. Patterson (2003)
J. Biol. Chem. 278, 49332-49341
   Abstract »    Full Text »    PDF »
The Tetraspanin CD81 Regulates the Expression of CD19 During B Cell Development in a Postendoplasmic Reticulum Compartment.
T. Shoham, R. Rajapaksa, C. Boucheix, E. Rubinstein, J. C. Poe, T. F. Tedder, and S. Levy (2003)
J. Immunol. 171, 4062-4072
   Abstract »    Full Text »    PDF »
An Intron Is Required for Dihydrofolate Reductase Protein Stability.
V. Noe, S. MacKenzie, and C. J. Ciudad (2003)
J. Biol. Chem. 278, 38292-38300
   Abstract »    Full Text »    PDF »
The Future of Regulatory Toxicology: Impact of the Biotechnology Revolution.
J. T. MacGregor (2003)
Toxicol. Sci. 75, 236-248
   Abstract »    Full Text »    PDF »
Dependence of Endoplasmic Reticulum-associated Degradation on the Peptide Binding Domain and Concentration of BiP.
M. Kabani, S. S. Kelley, M. W. Morrow, D. L. Montgomery, R. Sivendran, M. D. Rose, L. M. Gierasch, and J. L. Brodsky (2003)
Mol. Biol. Cell 14, 3437-3448
   Abstract »    Full Text »    PDF »
Overexpression of the Cochaperone CHIP Enhances Hsp70-Dependent Folding Activity in Mammalian Cells.
H. H. Kampinga, B. Kanon, F. A. Salomons, A. E. Kabakov, and C. Patterson (2003)
Mol. Cell. Biol. 23, 4948-4958
   Abstract »    Full Text »    PDF »
Relaxin increases ubiquitin-dependent degradation of fibronectin in vitro and ameliorates renal fibrosis in vivo.
G. A. McDonald, P. Sarkar, H. Rennke, E. Unemori, R. Kalluri, and V. P. Sukhatme (2003)
Am J Physiol Renal Physiol 285, F59-F67
   Abstract »    Full Text »    PDF »
Nucleolar localization of RPS19 protein in normal cells and mislocalization due to mutations in the nucleolar localization signals in 2 Diamond-Blackfan anemia patients: potential insights into pathophysiology.
L. Da Costa, G. Tchernia, P. Gascard, A. Lo, J. Meerpohl, C. Niemeyer, J.-A. Chasis, J. Fixler, and N. Mohandas (2003)
Blood 101, 5039-5045
   Abstract »    Full Text »    PDF »
The role of disulfide bonds in the assembly and function of MD-2.
G. E. D. Mullen, M. N. Kennedy, A. Visintin, A. Mazzoni, C. A. Leifer, D. R. Davies, and D. M. Segal (2003)
PNAS 100, 3919-3924
   Abstract »    Full Text »    PDF »
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad.
P. M. Quigley, K. Korotkov, F. Baneyx, and W. G. J. Hol (2003)
PNAS 100, 3137-3142
   Abstract »    Full Text »    PDF »
MecA, an adaptor protein necessary for ClpC chaperone activity.
T. Schlothauer, A. Mogk, D. A. Dougan, B. Bukau, and K. Turgay (2003)
PNAS 100, 2306-2311
   Abstract »    Full Text »    PDF »
Crystal Structure of the Protease Domain of a Heat-shock Protein HtrA from Thermotoga maritima.
D. Y. Kim, D. R. Kim, S. C. Ha, N. K. Lokanath, C. J. Lee, H.-Y. Hwang, and K. K. Kim (2003)
J. Biol. Chem. 278, 6543-6551
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Characterization of a Novel Intracellular Endopeptidase of the {alpha}/{beta} Hydrolase Family from Streptomyces coelicolor A3(2).
I. Nagy, T. Banerjee, T. Tamura, G. Schoofs, A. Gils, P. Proost, N. Tamura, W. Baumeister, and R. De Mot (2003)
J. Bacteriol. 185, 496-503
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Intracellular Accumulation of Antithrombin Morioka (C95R), a Novel Mutation Causing Type I Antithrombin Deficiency.
Y. Tanaka, K. Ueda, T. Ozawa, N. Sakuragawa, S. Yokota, R. Sato, S. Okamura, M. Morita, and T. Imanaka (2002)
J. Biol. Chem. 277, 51058-51067
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Structure-function analysis of the glucose-6-phosphate transporter deficient in glycogen storage disease type Ib.
L.-Y. Chen, C.-J. Pan, J.-J. Shieh, and J. Y. Chou (2002)
Hum. Mol. Genet. 11, 3199-3207
   Abstract »    Full Text »    PDF »
Eubacterial HslV and HslU Subunits Homologs in Primordial Eukaryotes.
B. Couvreur, R. Wattiez, A. Bollen, P. Falmagne, D. Le Ray, and J.-C. Dujardin (2002)
Mol. Biol. Evol. 19, 2110-2117
   Abstract »    Full Text »    PDF »


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