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SUMMARY:Structural Mechanisms in the Tyrosine Kinases that Initiate Immuno
 logical Signaling - Professor John Kuriyan\, University of California
DTSTART:20150521T151500Z
DTEND:20150521T161500Z
UID:TALK59394@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The activation of B- and T-lymphocytes relies on a chain of ty
 rosine phosphorylation events initiated by B-cell and T-cell receptors\, r
 espectively. These phosphorylation-dependent signals are generated by thre
 e kinds of non-receptor tyrosine kinases\, linked to the receptor by membr
 ane co-localization. Src-family kinases (principally Lyn and Fyn in B-cell
 s\, Lck and Fyn in T-cells)\, resident at the plasma membrane\, respond fi
 rst 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 Z
 AP-70 (in T-cells). Membrane localization of Syk or ZAP-70 leads to the re
 cruitment and activation of Tec-family tyrosine kinases\, Btk (in B-cells)
  and Itk (in T-cells). In this lecture I shall describe structural and mec
 hanistic studies aimed at understanding how these kinases are regulated.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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