Nucleocytoplasmic trafficking of macromolecules and heat shock proteins are key elements of the stress response; the analysis of nuclear transport and hsp70s will therefore contribute significantly to our understanding of cell physiology. / To study the formation of the Ran/Gsp1p nucleocytoplasmic gradient, an essential component of many nuclear transport reactions, I have used mutant strains of the yeast Saccharomyces cerevisiae. My experiments have identified the nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p and the enzyme acetyl-CoA carboxylase (MTR7) as proteins that regulate the distribution and cellular concentration of Ran/Gsp1p. Moreover, I have defined the mechanisms that underlie the control of the Ran/Gsplp gradient formation by these factors. / Using HeLa cells as a model system, I have demonstrated that the C-terminal part of mammalian hsc73 contains a unique targeting signal that is necessary and sufficient for stress-induced nuclear accumulation. This C-terminal segment promotes shuttling between nucleus and cytoplasm and has unique requirements for stress-dependent nuclear import.
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.80271 |
Date | January 2003 |
Creators | Gao, Huanhuan, 1974- |
Contributors | Stochaj, Ursula (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 Physiology.) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 002032368, proquestno: AAIMQ98640, Theses scanned by UMI/ProQuest. |
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