The activation of the protein tyrosine kinase (PTK) ZAP-70 is fundamental to T cell receptor (TCR) signal transduction. TCR engagement induces raft-association of ZAP-70 and juxtaposes the cytoplasmic ZAP-70 with the raft-enriched Lck, which phosphorylates and activates ZAP-70. The active ZAP-70, cooperatively with Lck, initiates multiple intracellular pathways eventually leading to T cell activation and IL-2 production. Here, we describe the serine phosphorylation on ZAP-70 on the highly conserved S520DVWS524 motif, and investigate its role in coupling ZAP-70 with TCR signal transduction.
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.19442 |
Date | January 2003 |
Creators | Yang, Yaoming |
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 | Doctor of Philosophy (Division of Experimental Medicine) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 002010389, Theses scanned by McGill Library. |
Page generated in 0.0018 seconds