Posttranslational quality control: Folding, refolding, and degrading proteins

Citation
S. Wickner et al., Posttranslational quality control: Folding, refolding, and degrading proteins, SCIENCE, 286(5446), 1999, pp. 1888-1893
Citations number
62
Categorie Soggetti
Multidisciplinary,Multidisciplinary,Multidisciplinary
Journal title
SCIENCE
ISSN journal
00368075 → ACNP
Volume
286
Issue
5446
Year of publication
1999
Pages
1888 - 1893
Database
ISI
SICI code
0036-8075(199912)286:5446<1888:PQCFRA>2.0.ZU;2-6
Abstract
Polypeptides emerging from the ribosome must fold into stable three-dimensi onal structures and maintain that structure throughout their functional Lif etimes. Maintaining quality control over protein structure and function dep ends on molecular chaperones and proteases, both of which can recognize hyd rophobic regions exposed on unfolded polypeptides. Molecular chaperones pro mote proper protein folding and prevent aggregation, and energy-dependent p roteases eliminate irreversibly damaged proteins. The kinetics of partition ing between chaperones and proteases determines whether a protein will be d estroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloi d diseases.