Regulation of CD3-induced phospholipase C-gamma1 (PLC gamma 1) tyrosine phosphorylation by CD4 and CD45 receptors

Stimulation of the signal transduction cascade in T cells through the T-cell receptor (CD3) coincides with activation of the phosphatidylinositol-phospholipase C (PI-PLC) pathway. Enzymatic activation of phospholipase C-gamma1 (PLC gamma 1) occurs through tyrosine phosphorylation in T cells followin...

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Bibliographic Details
Published in:Immunology 1992, Vol.75 (3), p.441-447
Main Authors: Kanner, S B, Deans, J P, Ledbetter, JA
Format: Article
Language:English
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Summary:Stimulation of the signal transduction cascade in T cells through the T-cell receptor (CD3) coincides with activation of the phosphatidylinositol-phospholipase C (PI-PLC) pathway. Enzymatic activation of phospholipase C-gamma1 (PLC gamma 1) occurs through tyrosine phosphorylation in T cells following surface ligation of CD3 receptors with CD3-specific monoclonal antibodies (mAb). Here we show that cross-linking of CD4 molecules with CD3 augments the tyrosine phosphorylation of PLC gamma 1, while co-ligation of CD3 with CD45 (a receptor tyrosine phosphatase) results in reduced PLC gamma 1 tyrosine phosphorylation. The observation that PLC gamma 1 exists in complexes with unique tyrosine phosphorylated proteins in T cells suggests that haematopoietic lineage-specific proteins associated with PLC gamma 1 may play roles in cellular signalling.
ISSN:0019-2805