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Structural Mechanisms in the Tyrosine Kinases that Initiate Immunological Signaling

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The activation of B- and T-lymphocytes relies on a chain of tyrosine phosphorylation events initiated by B-cell and T-cell receptors, respectively. These phosphorylation-dependent signals are generated by three kinds of non-receptor tyrosine kinases, linked to the receptor by membrane co-localization. Src-family kinases (principally Lyn and Fyn in B-cells, Lck and Fyn in T-cells), resident at the plasma membrane, respond first to receptor activation. They phosphorylate pairs of tyrosine residues in ITAM motifs in the cytoplasmic tails of activated receptors, which in turn recruit the tandem-SH2 domain tyrosine kinases Syk (in B-cells) and ZAP -70 (in T-cells). Membrane localization of Syk or ZAP -70 leads to the recruitment and activation of Tec-family tyrosine kinases, Btk (in B-cells) and Itk (in T-cells). In this lecture I shall describe structural and mechanistic studies aimed at understanding how these kinases are regulated.

This talk is part of the MRC LMB Seminar Series series.

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