Focal adhesion kinase modulates B cell receptor-transduced apoptosis in WEHI 231 cells

Abstract

B cell receptor (BCR) cross-linking induces tyrosine phosphorylation and activation of focal adhesion kinase (FAK), suggesting the role of this molecule in BCR-transduced signaling. The nature of FAK function in BCR-induced apoptosis of WEHI 231 lymphoblastoid cells was studied by overexpressing a C-terminal non-catalytic domain of FAK, termed focal adhesion targeted (FAT) domain. Clones overexpressing FAT protein exhibited a modified ability of induction of programmed cell death at low concentration threshold of anti-IgM antibodies, suggesting that FAK may play a role in modulating IgM-induced apoptotic signaling.