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The Journal of Immunology, 1999, 163: 1853-1858.
Copyright © 1999 by The American Association of Immunologists

Phospho-LAT-Independent Activation of the Ras-Mitogen-Activated Protein Kinase Pathway: A Differential Recruitment Model of TCR Partial Agonist Signaling1

Luan A. Chau* and Joaquín Madrenas2,*,{dagger}

* Transplantation and Immunobiology Group, John P. Robarts Research Institute, and {dagger} Departments of Microbiology and Immunology and of Medicine, University of Western Ontario, London, Ontario, Canada

Stimulation of mature T cells with agonist ligands of the Ag receptor (TCR) causes rapid phosphorylation of tyrosine-based activation motifs in the intracellular portion of TCR-{zeta} and CD3 and activation of several intracellular signaling cascades. Coordinate activation of these pathways is dependent on Lck- and ZAP-70-mediated tyrosine phosphorylation of a 36-kDa linker for activation of T cells and subsequent recruitment of phospholipase C-{gamma}1, Grb2-SOS, and SLP-76-vav. Here, we show that TCR partial agonist ligands can selectively activate one of these pathways, the Ras-mitogen-activated protein kinase pathway, by inducing recruitment of Grb2-SOS complexes to incompletely phosphorylated p21 phospho-TCR-{zeta}. This bypasses the need for activation of Lck and ZAP-70, and for phosphorylation of the linker for activation of T cells to activate Ras. We propose a general model in which differential recruitment of activating complexes away from transmembrane linker proteins may determine selective activation of a given signaling pathway.




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