Protein Disulfide Isomerase Superfamily in Disease and the Regulation of Apoptosis

• Authors: C. Grek , D.M. Townsend
• Languages of publication: EN

Abstracts

EN

Cellular homeostasis requires the balance of a multitude of signaling cascades that are contingent upon the essential proteins being properly synthesized, folded and delivered to appropriate subcellular locations. In eukaryotic cells the endoplasmic reticulum (ER) is a specialized organelle that is the central site of synthesis and folding of secretory, membrane and a number of organelletargeted proteins. The integrity of protein folding is enabled by the presence of ATP, Ca++, molecular chaperones, as well as an oxidizing redox environment. The imbalance between the load and capacity of protein folding results in a cellular condition known as ER stress. Failure of these pathways to restore ER homeostasis results in the activation of apoptotic pathways. Protein disulfide isomerases (PDI) compose a superfamily of oxidoreductases that have diverse sequences and are localized in the ER, nucleus, cytosol, mitochondria and cell membrane. The PDI superfamily has multiple functions including, acting as molecular chaperones, protein-binding partners, and hormone reservoirs. Recently , PDI family members have been implicated in the regulation of apoptotic signaling events. The complexities underlying the molecular mechanisms that define the switch from pro-survival to pro-death response are evidenced by recent studies that reveal the roles of specific chaperone proteins as integration points in signaling pathways that determine cell fate. The following review discusses the dual role of PDI in cell death and survival during ER stress.

Keywords

EN

PDI; ER; ER stress; Apoptosis; Misfolded proteins; UPR; Oxidative stress; Redox; Conformational disease

• Publisher: De Gruyter Open
• Journal: Endoplasmic Reticulum Stress in Diseases
• Year: 2014
• Volume: 1
• Issue: 1

Dates

published

1 - 1 - 2014

received

2 - 2 - 2013

online

25 - 4 - 2013

accepted

27 - 2 - 2013

Contributors

author

C. Grek

• Department of Cell and Molecular Pharmacology and Experimental Therapeutics

author

D.M. Townsend

• Drug Discovery and Biomedical Sciences, Medical University of South Carolina, Charleston, SC 29425

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Identifiers

DOI

10.2478/ersc-2013-0001