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 CD3zeta. 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.
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|Titolo:||Temporally regulated assembly of a dynamic signaling complex associated with the activated TCR|
|Rivista:||EUROPEAN JOURNAL OF IMMUNOLOGY|
|Citazione:||Pacini, S., Valensin, S., Telford, J.l., Laadbury, J., & Baldari, C. (2000). Temporally regulated assembly of a dynamic signaling complex associated with the activated TCR. EUROPEAN JOURNAL OF IMMUNOLOGY, 30, 2620-2631.|
|Appare nelle tipologie:||1.1 Articolo in rivista|
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