Quality control in the endoplasmic reticulum: crosstalk between ERAD and UPR pathways

J Hwang, L Qi - Trends in biochemical sciences, 2018 - cell.com
Endoplasmic reticulum (ER)-associated degradation (ERAD) and the unfolded protein
response (UPR) are two key quality-control machineries in the cell. ERAD is responsible for …

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends

KFR Pobre, GJ Poet, LM Hendershot - Journal of Biological Chemistry, 2019 - ASBMB
The endoplasmic reticulum (ER) represents the entry point into the secretory pathway where
nascent proteins encounter a specialized environment for their folding and maturation …

Glycosylation-directed quality control of protein folding

C Xu, DTW Ng - Nature reviews Molecular cell biology, 2015 - nature.com
Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated
in the endoplasmic reticulum. These adducts have many biological functions, including …

Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system

J Verghese, J Abrams, Y Wang… - … and molecular biology …, 2012 - Am Soc Microbiol
The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

Regulation of calcium homeostasis and flux between the endoplasmic reticulum and the cytosol

L Daverkausen-Fischer, F Pröls - Journal of Biological Chemistry, 2022 - ASBMB
The concentration of Ca 2+ in the endoplasmic reticulum (ER) is critically important for
maintaining its oxidizing environment as well as for maintaining luminal ATP levels required …

BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions

J Behnke, MJ Feige, LM Hendershot - Journal of molecular biology, 2015 - Elsevier
BiP (immunoglobulin heavy-chain binding p rotein) is the endoplasmic reticulum (ER)
orthologue of the Hsp70 family of molecular chaperones and is intricately involved in most …

Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope

AB Mehrtash, M Hochstrasser - Seminars in cell & developmental biology, 2019 - Elsevier
Numerous nascent proteins undergo folding and maturation within the luminal and
membrane compartments of the endoplasmic reticulum (ER). Despite the presence of …

[HTML][HTML] Mechanisms of productive folding and endoplasmic reticulum-associated degradation of glycoproteins and non-glycoproteins

S Ninagawa, G George, K Mori - … et biophysica acta (BBA)-General subjects, 2021 - Elsevier
Background The quality of proteins destined for the secretory pathway is ensured by two
distinct mechanisms in the endoplasmic reticulum (ER): productive folding of newly …

Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems

JL Brodsky, WR Skach - Current opinion in cell biology, 2011 - Elsevier
The evolution of eukaryotes was accompanied by an increased need for intracellular
communication and cellular specialization. Thus, a more complex collection of secreted and …

Chaperoning endoplasmic reticulum–associated degradation (ERAD) and protein conformational diseases

PG Needham, CJ Guerriero… - Cold Spring Harbor …, 2019 - cshperspectives.cshlp.org
Misfolded proteins compromise cellular homeostasis. This is especially problematic in the
endoplasmic reticulum (ER), which is a high-capacity protein-folding compartment and …