Quality Control of Protein Folding in the Cytosol
Date
2012-05
Authors
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Publisher
Wilvey
Abstract
In order to function properly, newly synthesised proteins
must rapidly and efficiently attain their native conformations. If they fail to do so, the cell may be adversely
affected due to loss of function or toxic gain of function
effects of misfolded polypeptides. Effective quality control mechanisms to recognise and eliminate misfolded
proteins are thus critical for cell viability.The primary
means by which misfolded proteins are selectively
removed from the cell is via the ubiquitin–proteasome
system. Although much is known about regulated proteolysis, how any given protein,which could potentially
misfold, is recognised and targeted for proteasome-mediated degradation has been challenging to decipher.
Recent progress,much of it in yeast, has identified specific
E3 ligases involved in this process,clarified or added to our
knowledge of the roles of molecular chaperones,and
identified multiple cellular locations where degradation,
or failing that, aggregation, occurs.
Description
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Keywords
Cell Biology, Cytology
Citation
McClellan, Amie J. (May 2012) Quality Control of Protein Folding in the Cytosol. In:eLS.John Wiley & Sons, Ltd:Chichester. DOI: 10.1002/9780470015902.a0020886.pub2