AI Article Synopsis
- Focal adhesion kinase (FAK) is crucial for cell signaling related to adhesion and has a docking site for various proteins, including Src-family kinases.
- In a study, expressing the N-terminal domain of FAK in breast cancer cells (BT474 and MCF-7) caused cell rounding, detachment, and apoptosis, linked to decreased FAK phosphorylation and caspase-3 activation.
- Unlike cancer cells, expressing FAK-NT in non-cancerous cells (MCF-10A) did not result in similar effects, indicating that FAK-NT is essential for adhesion and survival specifically in breast cancer cells.
Article 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 Tyr(397), 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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223465 | PMC |
| http://dx.doi.org/10.1042/BJ20021846 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!