To understand the physiological role of the protein tyrosine phosphatase (PTP) PEST, the phenotypes of PTP-PEST (--/--) mouse fibroblasts have been studied PTP-PEST was shown to translocate to the membrane periphery following stimulation by the extracellular matrix protein fibronectin, and to play a role in cell migration, spreading, and cytokinesis. For this action, PTP-PEST was shown to regulate the phosphorylation levels of p130cas, paxillin, FAK and PSTPIP, and their association with SH2 domain-containing proteins like Src and Crk. From these proteins, p130cas is known to be a direct substrate. Experiments for the obtention of p130cas (--/--) embryos and cell lines have also been initiated, up to the generation of adult chimeric animals. In the process, a genomic fragment of p130cas containing a C-terminal exon has been cloned and analysed.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.21504 |
| Date | January 1999 |
| Creators | Angers-Loustau, Alexandre. |
| Contributors | Tremblay, Michel L. (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 Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001652042, proquestno: MQ50710, Theses scanned by UMI/ProQuest. |
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