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Updated: Aug 8, 2026

A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins
Published on: March 22, 2012
B cell receptor signaling involves physical and functional association of FAK with Lyn and IgM
I Mlinaric-Rascan1, T Yamamoto
1Department of Oncology, Institute of Medical Science, University of Tokyo, Japan.
Abstract:
B cell receptor (BCR) stimulation induces phosphorylation of a number of proteins, leading to functional activation of B lymphocytes. Focal adhesion kinase (FAK) is a non-receptor protein tyrosine kinase, involved in a variety of signaling pathways. In this study, we show that FAK is tyrosine-phosphorylated and activated following BCR stimulation. We also demonstrate constitutive association of FAK with the Src-family kinase Lyn and with components of the BCR. Association of Lyn with FAK which was not correlated with BCR-induced activation of both kinases, appeared to be mediated via the binding of Lyn to the COOH-terminal part of the FAK molecule. Our results indicate that FAK is a component of the BCR complex and that it participates in BCR signaling.
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