Regulation of src family tyrosine kinases in lymphocytes

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Abstract

An immune response is initiated by activation of antigen-specific lymphoid cells via receptors on the cell surface. Recent advances have begun to unravel the molecular pathways by which the signals from these surface receptors are transduced into the cells and affect the cell's behavior. Phosphorylation of key regulatory proteins on specific tyrosine residues is emerging as a central mechanism to activate, modulate or translocate these regulatory proteins. In this review, we summarize the current picture on the role and regulation of the src family of protein tyrosine kinases thought to be involved in lymphocyte activation, and put forward a working hypothesis that might serve as a basis for further experimentation.

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      CD45 is a prototypic transmembrane protein tyrosine phosphatase (PTP), and it is generally accepted today that it sets the threshold of positive and negative signaling events in leukocytes.12-15 Through dephosphorylation and activation of the src-family kinases Lck, Fyn, and Lyn, CD45 is a positive regulator for signaling via the T-cell and B-cell receptors, respectively.16-18 On the other hand, through dephosphorylation of JAK, CD45 has been shown to negatively regulate cytokine receptor signaling and promotes viral infections.19

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