Protein Quality Control in the Endoplasmic Reticulum

Overview

Journal F1000Prime Rep

Specialty Biomedical Engineering

Date 2014 Sep 4

PMID 25184039

Citations 6

Authors

Paul-Albert Koenig

Hidde L Ploegh

Affiliations

Soon will be listed here.

Abstract

THE TOPOLOGICAL BARRIERS DEFINED BY BIOLOGICAL MEMBRANES ARE NOT IMPERMEABLE: from small solutes to intact proteins, specialized transport and translocation mechanisms adjust to the cell's needs. Here, we review the removal of unwanted proteins from the endoplasmic reticulum (ER) and emphasize the need to extend observations from tissue culture models and simple eukaryotes to studies in whole animals. The variation in protein production and composition that characterizes different cell types and tissues requires tailor-made solutions to exert proper control over both protein synthesis and breakdown. The ER is an organelle essential to achieve and maintain such homeostasis.

Citing Articles

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Transmembrane domain quality control systems operate at the endoplasmic reticulum and Golgi apparatus.

Briant K, Johnson N, Swanton E PLoS One. 2017; 12(4):e0173924.

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Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e.

Hagiwara M, Ling J, Koenig P, Ploegh H Mol Cell. 2016; 63(5):753-67.

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