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• W1965521568 startingPage "26" @default.
• W1965521568 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." @default.
• W1965521568 created "2016-06-24" @default.
• W1965521568 creator A5024136589 @default.
• W1965521568 creator A5081865434 @default.
• W1965521568 date "2001-05-30" @default.
• W1965521568 modified "2023-10-14" @default.
• W1965521568 title "B cell receptor signaling involves physical and functional association of FAK with Lyn and IgM" @default.
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• W1965521568 doi "https://doi.org/10.1016/s0014-5793(01)02474-7" @default.
• W1965521568 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11389892" @default.
• W1965521568 hasPublicationYear "2001" @default.
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