Sorting Out the Trash: The Spatial Nature of Eukaryotic Protein Quality Control

Authors

Emily M. Sontag, Marquette UniversityFollow
Willianne IM Vonk, Stanford University
Judith Frydman, Stanford University

Document Type

Article

Publication Date

2-2014

Publisher

Elsevier

Source Publication

Current Opinion in Cell Biology

Source ISSN

0955-0674

Original Item ID

DOI: 10.1016/j.ceb.2013.12.006

Abstract

Failure to maintain protein homeostasis is associated with aggregation and cell death, and underlies 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.

Comments

Accepted version. Current Opinion in Cell Biology, Vol. 26 (February 2014): 139-146. DOI. © 2014 Elsevier. Used with permission.

Recommended Citation

Sontag, Emily M.; Vonk, Willianne IM; and Frydman, Judith, "Sorting Out the Trash: The Spatial Nature of Eukaryotic Protein Quality Control" (2014). Biological Sciences Faculty Research and Publications. 937.
https://epublications.marquette.edu/bio_fac/937