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Oxygen is required to retain Ero1α on the MAM Open Access


Other title
oxidative protein folding
Type of item
Degree grantor
University of Alberta
Author or creator
Gilady, Susanna
Supervisor and department
Dr. Simmen, Thomas (Cell Biology)
Examining committee member and department
Dr. Baksh, Shairaz (Pediatrics)
Dr. Eitzen, Gary (Cell Biology)
Department of Cell Biology

Date accepted
Graduation date
Master of Science
Degree level
Oxidative protein folding within the ER depends on the enzymatic action of numerous chaperones and oxidoreductases. In addition, this process requires the influx of metabolites and energy, including FAD (flavin adenine dinucleotide) and molecular oxygen. Secretory proteins and proteins destined to the secretory pathway need to undergo this process in order to obtain stability and full functionality. Since secretory proteins that fail to fully fold are eliminated by degradation, the process of ER oxidative protein folding is part of a group of ER-associated mechanisms commonly referred to as ER quality control. Interestingly, the proteins that mediate ER quality control can be found in a variety of diverse subdomains of the ER. We have found that the ER-oxidoreductase Ero1α is located on the mitochondria-associated-membrane, the MAM. This specialized subdomain of the ER has been shown to be crucial for a number of processes such as the synthesis of phospholipids as well as calcium-channelling between the ER and mitochondria. The goal of this thesis was to identify possible retention mechanisms and motifs of Ero1α to the MAM.
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