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Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process

This article discusses current knowledge of the ER and mitochondria, including their functional similarities and differences. The endoplasmic reticulum (ER) was long considered to be the only compartment of the eukaryotic cell in which protein folding is accompanied by enzyme-catalyzed disulfide bond formation. However, it has recently become evident that cells harbor a second oxidizing compartment, the mitochondrial intermembrane space, where disulfide formation facilitates protein translocation from the cytosol. Moreover, protein oxidation has been implicated in many mitochondria-associated processes central for human health such as apoptosis, aging, and regulation of the respiratory chain. Whereas the machineries of ER and mitochondria both form disulfides between cysteine residues, they do not share evolutionary origins and exhibit distinct mechanistic properties. Here, we summarize the current knowledge of these oxidation systems and discuss their functional similarities and differences.

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Classifications


Resource Type: Journal article/Issue, Illustration, Review
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Professional (degree program), Continuing education

Author and Copyright


Authors and Editors: Jan Riemer of Cell Biology, University of Kaiserslautern, Neil Bulleid of Faculty of Life Sciences, University of Manchester, Johannes M. Herrmann of Cell Biology, University of Kaiserslautern
Publisher: SCIENCE
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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Collection:
American Association for the Advancement of Science


     
   

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