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Permanent link (DOI): https://doi.org/10.7939/R31M0C

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Oxygen is required to retain Ero1α on the MAM Open Access

Descriptions

Other title
Subject/Keyword
oxidative protein folding
Type of item
Thesis
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
Department of Cell Biology
Specialization

Date accepted
2009-10-01T18:05:01Z
Graduation date
2009-11
Degree
Master of Science
Degree level
Master's
Abstract
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.
Language
English
DOI
doi:10.7939/R31M0C
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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