In response to stresses such as the accumulation of misfolded proteins, the Endoplasmic Reticulum (ER) triggers cytosolic and nuclear signalling events, which are integrated by the cell to result in adaptation or apoptosis. The activation of stress-responsive kinases (SAPKs) and the mitogen-activated kinases (MAPKs) are known to have a key influence cell fate determination. We developed a technique to study the regulation of these kinases by the ER in response to drugs inducing protein misfolding. We isolated ER like compartments with a relatively high degree of purity using magnetic beads coated with anti-calnexin antibodies and vie reconstituted in a cell free system the ER signalling induced by different stresses. We demonstrate here that ER-like compartments isolated from cells treated with azetidine-2 carboxylic acid or Tunicamycin differentially activates ERK-1, JNK-1 and p38 in vitro. Moreover, we show that the molecular adaptors Shc and Nck are involved in the ER-mediated regulation of these kinases.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.79117 |
| Date | January 2002 |
| Creators | Rousselle, Etienne |
| Contributors | Bergeron, John J. M. (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Anatomy and Cell Biology.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001974964, proquestno: AAIMQ88286, Theses scanned by UMI/ProQuest. |
Page generated in 0.0031 seconds