Molecular mechanisms of Lck activity regulation in human peripheral blood T lymphocytes
Irles C., Ortega A., Michel F., Acuto O.
Lck activation during T cell signaling is still not completely understood. In order to study this regulation in more physiologic stimulation conditions, we used resting human peripheral blood CD4(+) lymphoblasts stimulated with SAg-loaded APC's. Here we show that dephosphorylation of its negative regulatory residue (Tyr505) is a pre-requisite for promoting phosphorylation of Tyr394 residue in the kinase domain further enhancing the activity of Lek.