FAK and p53 protein interactions.

Abstract

Focal Adhesion Kinase plays a major role in cell adhesion, motility, survival, proliferation, metastasis, angiogenesis and lymphangiogenesis. In 2004, we have cloned the promoter sequence of FAK and found that p53 inhibits its activity (BBA, v. 1678, 2004). In 2005, we were the first group to show that FAK and p53 proteins directly interact in the cells (JBC, v. 280, 2005). We have shown that FAK and p53 proteins interact in the cytoplasm and in the nucleus by immunoprecipitation, pull-down and confocal microscopy assays. We have shown that FAK inhibited activity of p53 with the transcriptional targets: p21, Bax and Mdm-2 through protein-protein interactions. We identified the 7 amino-acid site in p53 that is involved in interaction with FAK protein. The present review will discuss the interaction of FAK and p53 proteins and discuss the mechanism of FAK-p53 loop regulation: inhibition of FAK promoter activity by p53 protein and also inhibition of p53 transcriptional activity by FAK protein.

• Authors: Vita M Golubovskaya, William G Cance
• Journal: Anti-cancer agents in medicinal chemistry (Anticancer Agents Med Chem) Vol. 11 Issue 7 Pg. 617-9 (Sep 2011) ISSN: 1875-5992 [Electronic] Netherlands
• PMID: 21355845 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)

Chemical References

• Tumor Suppressor Protein p53
• Focal Adhesion Protein-Tyrosine Kinases

Topics

• Apoptosis
• Cell Survival
• Feedback, Physiological
• Focal Adhesion Protein-Tyrosine Kinases (genetics, metabolism)
• Gene Expression Regulation, Neoplastic
• Humans
• Neoplasms (genetics, metabolism, pathology)
• Promoter Regions, Genetic
• Protein Binding
• Protein Interaction Mapping
• Protein Structure, Tertiary
• Signal Transduction
• Transcriptional Activation
• Tumor Suppressor Protein p53 (genetics, metabolism)