Mechanisms and Functions of Spatial Protein Quality Control

Authors

Emily M. Sontag, Marquette UniversityFollow
Rahul S. Samant, Stanford University
Judith Frydman, Stanford University

Document Type

Article

Publication Date

6-2017

Publisher

Annual Reviews

Source Publication

Annual Review of Biochemistry

Source ISSN

0066-4154

Original Item ID

DOI: 10.1146/annurev-biochem-060815-014616

Abstract

A healthy proteome is essential for cell survival. Protein misfolding is linked to a rapidly expanding list of human diseases, ranging from neurodegenerative diseases to aging and cancer. Many of these diseases are characterized by the accumulation of misfolded proteins in intra- and extracellular inclusions, such as amyloid plaques. The clear link between protein misfolding and disease highlights the need to better understand the elaborate machinery that manages proteome homeostasis, or proteostasis, in the cell. Proteostasis depends on a network of molecular chaperones and clearance pathways involved in the recognition, refolding, and/or clearance of aberrant proteins. Recent studies reveal that an integral part of the cellular management of misfolded proteins is their spatial sequestration into several defined compartments. Here, we review the properties, function, and formation of these compartments. Spatial sequestration plays a central role in protein quality control and cellular fitness and represents a critical link to the pathogenesis of protein aggregation-linked diseases.

Comments

Accepted version. Annual Review of Biochemistry, Vol. 86 (June 2017): 97-122. DOI. © 2017 Annual Reviews of Biochemistry. Used with permission.

Recommended Citation

Sontag, Emily M.; Samant, Rahul S.; and Frydman, Judith, "Mechanisms and Functions of Spatial Protein Quality Control" (2017). Biological Sciences Faculty Research and Publications. 942.
https://epublications.marquette.edu/bio_fac/942