@article{1c1c632c78a94c8daf8ebfbe9ef99723,
title = "Focal adhesion kinase N-terminus in breast carcinoma cells induces rounding, detachment and apoptosis",
abstract = "Focal adhesion kinase (FAK) has a central role in adhesion-mediated cell signalling. The N-terminus of FAK is thought to function as a docking site for a number of proteins, including the Src-family tyrosine kinases. In the present study, we disrupted FAK signalling by expressing the N-terminal domain of FAK (FAK-NT) in human breast carcinoma cells, BT474 and MCF-7 lines, and non-malignant epithelial cells, MCF-10A line. Expression of FAK-NT led to rounding, detachment and apoptosis in human breast cancer cells. Apoptosis was accompanied by dephosphorylation of FAK Tyr397, degradation of the endogenous FAK protein and activation of caspase-3. Over-expression of FAK rescued FAK-NT-mediated cellular rounding. Expression of FAK-NT in non-malignant breast epithelial cells did not lead to rounding, loss of FAK phosphorylation or apoptosis. Thus FAK-NT contributes to cellular adhesion and survival pathways in breast cancer cells which are not required for survival in non-malignant breast epithelial cells.",
keywords = "Apoptosis, Breast cancer cell, Caspase activation, Protein degradation",
author = "Lucia Beviglia and Vita Golubovskaya and Xu, \{Li Hui\} and Yang, \{Xi Hui\} and Craven, \{Rolf J.\} and Cance, \{William G.\}",
year = "2003",
month = jul,
day = "1",
doi = "10.1042/BJ20021846",
language = "English",
volume = "373",
pages = "201--210",
number = "1",
}
