scholarly journals Cysteine sulfenic Acid as an Intermediate in Disulfide Bond Formation and Nonenzymatic Protein Folding

Biochemistry ◽  
2010 ◽  
Vol 49 (35) ◽  
pp. 7748-7755 ◽  
Author(s):  
Douglas S. Rehder ◽  
Chad R. Borges
Keyword(s):  
Protein Folding ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Sulfenic Acid

355 HYPOXIA INHIBITS DISULFIDE BOND FORMATION AND PROTEIN FOLDING IN THE ENDOPLASMIC RETICULUM

2012 ◽  
Vol 102 ◽  
pp. S185-S186
Author(s):  
M. Koritzinsky ◽  
T. Van den Beucken ◽  
K. Chu ◽  
P.C. Boutros ◽  
I. Braakman ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation

scholarly journals From recordings of disulfide isomerases in action to reversal of maladaptive endoplasmic reticulum stress responses: proceedings on the ER & Redox Club Meeting held in Venice, April 2015

2015 ◽  
Vol 2 (1) ◽  
Author(s):  
Eelco van Anken
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Disulfide Bond ◽  
Stress Responses ◽  
Bond Formation ◽  
Genetic Defect ◽  
Cell Protein ◽  
Disulfide Bond Formation ◽  
Club Meeting ◽  
Client Proteins

AbstractThe endoplasmic reticulum (ER) interacts and cooperates with other organelles as a central hub in cellular homeostasis. In particular, the ER is the first station along the secretory pathway, where client proteins fold and assemble before they travel to their final destination elsewhere in the endomembrane system or outside the cell. Protein folding and disulfide bond formation go hand in hand in the ER, a task that is achieved with the help of ER-resident chaperones and other folding factors, including oxidoreductases that catalyze disulfide bond formation. Yet, when their combined effort is in vain, client proteins that fail to fold are disposed of through ER-associated degradation (ERAD). The ER folding and ERAD machineries can be boosted through the unfolded protein response (UPR) if required. Still, protein folding in the ER may consistently fail when proteins are mutated due to a genetic defect, which, ultimately, can lead to disease. Novel developments in all these fields of study and how new insights ultimately can be exploited for clinical or biotechnological purposes were highlighted in a rich variety of presentations at the ER & Redox Club Meeting that was held in Venice from 15 to 17 April 2015. As such, the meeting provided the participants an excellent opportunity to mingle and discuss key advancements and outstanding questions on ER function in health and disease.

scholarly journals PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

Molecules ◽  
2020 ◽  
Vol 26 (1) ◽  
pp. 171
Author(s):  
Jiahui Fu ◽  
Jihui Gao ◽  
Zhongxin Liang ◽  
Dong Yang
Keyword(s):  
Protein Folding ◽  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Protein Disulfide Isomerase ◽  
Bond Formation ◽  
Molecular Assembly ◽  
Disulfide Bond Formation ◽  
Disulfide Isomerase ◽  
Biomolecular Assembly ◽  
Protein Disulfide

Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the intermolecular crosslinking via disulfide bonds. In eukaryotes, the formation and rearrangement of most intra- and intermolecular disulfide bonds in the endoplasmic reticulum (ER) are mediated by protein disulfide isomerases (PDIs), which consist of multiple thioredoxin-like domains. These domains assist correct folding of proteins, as well as effectively prevent the aggregation of misfolded ones. Protein misfolding often leads to the formation of pathological protein aggregations that cause many diseases. On the other hand, glutenin aggregation and subsequent crosslinking are required for the formation of a rheologically dominating gluten network. Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly. This review systematically illustrated the process of human protein disulfide isomerase (hPDI) mediated disulfide bond formation and complemented this with the current mechanism of wheat protein disulfide isomerase (wPDI) catalyzed formation of gluten networks.

Sign in / Sign up

Export Citation Format

Share Document