Temporally regulated assembly of a dynamic signaling complex associated with the activated TCR
暂无分享,去创建一个
TCR triggering promotes multiple tyrosine kinase‐dependent interactions involving proteins with one or more protein binding modules. Reported interactions mostly exceed the binding potential of these proteins. A solution to this paradox is the temporally regulated recruitment of alternative ligands. We have tested this hypothesis by analyzing the time course of protein/protein interactions triggered by TCR engagement. We show that a short‐lived and dynamic multimolecular complex is assembled on tyrosine‐phosphorylated CD3ζ. Specific components of this complex are recruited and shed in a temporal sequence distinct for each of the proteins analyzed. The temporally regulated assembly of a higher order structure at the activated TCR is likely to be crucial in achieving both signal longevity and signal specificity.