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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.

Type

Conference paper

Publication Date

2004

Pages

163 - 167

Keywords

lipid rafts, PROTEIN-TYROSINE KINASE, CELL-ACTIVATION, ENRICHED MICRODOMAINS, CSK, FYN