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Curr Opin Cell Biol. 2014 Feb;26:139-146. doi: 10.1016/j.ceb.2013.12.006. Epub 2014 Jan 23.

Sorting out the trash: the spatial nature of eukaryotic protein quality control.

Author information

1
Department of Biology, Stanford University, Stanford, California 94305, USA.
#
Contributed equally

Abstract

Failure to maintain protein homeostasis is associated with aggregation and cell death, and underies a growing list of pathologies including neurodegenerative diseases, aging, and cancer. Misfolded proteins can be toxic and interfere with normal cellular functions, particularly during proteotoxic stress. Accordingly, molecular chaperones, the ubiquitin-proteasome system (UPS) and autophagy together promote refolding or clearance of misfolded proteins. Here we discuss emerging evidence that the pathways of protein quality control (PQC) are intimately linked to cell architecture, and sequester proteins into spatially and functionally distinct PQC compartments. This sequestration serves a number of functions, including enhancing the efficiency of quality control; clearing the cellular milieu of potentially toxic species and facilitating asymmetric inheritance of damaged proteins to promote rejuvenation of daughter cells.

PMID:
24463332
PMCID:
PMC4204729
DOI:
10.1016/j.ceb.2013.12.006
[Indexed for MEDLINE]
Free PMC Article

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