Cellular Strategies of Protein Quality Control
Author(s) -
Bo Chen,
Marco Retzlaff,
Thomas R. Roos,
Judith Frydman
Publication year - 2011
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a004374
Subject(s) - biology , protein folding , proteome , protein quality , microbiology and biotechnology , protein aggregation , proteostasis , computational biology , co chaperone , cell , chaperone (clinical) , bioinformatics , biochemistry , gene , heat shock protein , hsp90 , medicine , pathology
Eukaryotic cells must contend with a continuous stream of misfolded proteins that compromise the cellular protein homeostasis balance and jeopardize cell viability. An elaborate network of molecular chaperones and protein degradation factors continually monitor and maintain the integrity of the proteome. Cellular protein quality control relies on three distinct yet interconnected strategies whereby misfolded proteins can either be refolded, degraded, or delivered to distinct quality control compartments that sequester potentially harmful misfolded species. Molecular chaperones play a critical role in determining the fate of misfolded proteins in the cell. Here, we discuss the spatial and temporal organization of cellular quality control strategies and their implications for human diseases linked to protein misfolding and aggregation.
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