Author/Editor		Mlinarič-Raščan, Irena; Yamamoto, Tadashi
Title		B cell receptor signaling involves physical and functional association of FAK with Lyn and IgM
Type		članek
Source		Febs Lett
Vol. and No.		Letnik 498, št. 1
Publication year		2001
Volume		str. 26-31
Language		eng
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.
Descriptors		B-LYMPHOCYTES IMMUNOGLOBULINS PROTEIN-TYROSINE KINASE RECEPTORS, ANTIGEN, B-CELL SRC-FAMILY KINASES ANTIGEN-ANTIBODY COMPLEX CELL LINE, TRANSFORMED CELLS, CULTURED MICE PHOSPHORYLATION PROTEIN STRUCTURE, TERTIARY SIGNAL TRANSDUCTION TYROSINE