Oxygen is required to retain Ero1α on the MAM

  • Author / Creator
    Gilady, Susanna
  • 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.

  • Subjects / Keywords
  • Graduation date
  • Type of Item
  • Degree
    Master of Science
  • DOI
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
  • Language
  • Institution
    University of Alberta
  • Degree level
  • Department
    • Department of Cell Biology
  • Supervisor / co-supervisor and their department(s)
    • Dr. Simmen, Thomas (Cell Biology)
  • Examining committee members and their departments
    • Dr. Baksh, Shairaz (Pediatrics)
    • Dr. Eitzen, Gary (Cell Biology)