ζ phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists
J Madrenas, RL Wange, JL Wang, N Isakov… - Science, 1995 - science.org
J Madrenas, RL Wange, JL Wang, N Isakov, LE Samelson, RN Germain
Science, 1995•science.orgSmall changes in the peptide-major histocompatibility complex (MHC) molecule ligands
recognized by antigen-specific T cell receptors (TCRs) can convert fully activating
complexes into partially activating or even inhibitory ones. This study examined early TCR-
dependent signals induced by such partial agonists or antagonists. In contrast to typical
agonist ligands, both an antagonist and several partial agonists stimulated a distinct pattern
of ζ chain phosphorylation and failed to activate associated ZAP-70 kinase. These results …
recognized by antigen-specific T cell receptors (TCRs) can convert fully activating
complexes into partially activating or even inhibitory ones. This study examined early TCR-
dependent signals induced by such partial agonists or antagonists. In contrast to typical
agonist ligands, both an antagonist and several partial agonists stimulated a distinct pattern
of ζ chain phosphorylation and failed to activate associated ZAP-70 kinase. These results …
Small changes in the peptide-major histocompatibility complex (MHC) molecule ligands recognized by antigen-specific T cell receptors (TCRs) can convert fully activating complexes into partially activating or even inhibitory ones. This study examined early TCR-dependent signals induced by such partial agonists or antagonists. In contrast to typical agonist ligands, both an antagonist and several partial agonists stimulated a distinct pattern of ζ chain phosphorylation and failed to activate associated ZAP-70 kinase. These results identify a specific step in the early tyrosine phosphorylation cascade that is altered after TCR engagement with modified peptide-MHC molecule complexes. This finding may explain the different biological responses to TCR occupancy by these variant ligands.
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