Structural Mechanisms in the Tyrosine Kinases that Initiate Immunological Signaling

Add to your list(s) Download to your calendar using vCal

• Professor John Kuriyan, University of California
• Thursday 21 May 2015, 16:15-17:15
• Max Perutz Lecture Theatre, Medical Research Council (MRC) (MRC Laboratory of Molecular Biol.

If you have a question about this talk, please contact Scientific Meetings Co-ordinator.

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.

This talk is included in these lists:

• All Talks (aka the CURE list)
• Biology
• CCC talks for website
• Cambridge Immunology
• Cambridge Infectious Diseases
• Centre for Health Leadership and Enterprise
• Liam
• Life Sciences
• Life Sciences
• ME Seminar
• MRC LMB Seminar Series
• Max Perutz Lecture Theatre, Medical Research Council (MRC) (MRC Laboratory of Molecular Biol
• Neurons, Fake News, DNA and your iPhone: The Mathematics of Information
• cri
• my_list
• other talks
• rc781

Note that ex-directory lists are not shown.