Görlach, Agnes and Klappa, Peter and Kietzmann, Thomas (2006) The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxidants and Redox Signaling, 8 (9-10). pp. 1391-418. ISSN 1557-7716. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
|The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)|
The endoplasmic reticulum (ER) plays a major role in regulating synthesis, folding, and orderly transport of proteins. It is also essentially involved in various cellular signaling processes, primarily by its function as a dynamic Ca(2+) store. Compared to the cytosol, oxidizing conditions are found in the ER that allow oxidation of cysteine residues in nascent polypeptide chains to form intramolecular disulfide bonds. However, compounds and enzymes such as PDI that catalyze disulfide bonds become reduced and have to be reoxidized for further catalytic cycles. A number of enzymes, among them products of the ERO1 gene, appear to provide oxidizing equivalents, and oxygen appears to be the final oxidant in aerobic living organisms. Thus, protein oxidation in the ER is connected with generation of reactive oxygen species (ROS). Changes in the redox state and the presence of ROS also affect the Ca(2+) homeostasis by modulating the functionality of ER-based channels and buffering chaperones. In addition, a close relationship exists between oxidative stress and ER stress, which both may activate signaling events leading to a rebalance of folding capacity and folding demand or to cell death. Thus, redox homeostasis appears to be a prerequisite for proper functioning of the ER.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Peter Klappa|
|Date Deposited:||29 Jun 2011 11:35|
|Last Modified:||22 Apr 2014 11:30|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/3965 (The current URI for this page, for reference purposes)|