XIAP reverses various functional activities of FRNK in endothelial cells

详细信息	查看全文 | 推荐本文 |

• 作者：Sunyoung Ahn^a ; Hyun Jeong Kim^a ; Sung-Gil Chi^b ; Heonyong Park^a ; ^{heonyong@dankook.ac.kr}
• 关键词：XIAP ; X-chromosome linked inhibitor of apoptosis protein ; FAK ; focal adhesion kinase ; FERM domain ; band 4.1 ; ezrin ; radixin ; moesin domain ; FAT ; focal adhesion targeting ; FRNK ; FAK-related non-kinase ; BAEC ; bovine aortic endothelial cell ; ERK ; extracellul
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：9 March, 2012
• 卷：419
• 期：2
• 页码：419-424
• 文件大小：570 K

摘要

In endothelial cells, focal adhesion kinase (FAK) regulates cell proliferation, migration, adhesion, and shear-stimulated activation of MAPK. We recently found that FAK is recruited into focal adhesion (FA) sites through interactions with XIAP (X-chromosome linked inhibitor of apoptosis protein) and activated by Src kinase in response to shear stress. In this study, we examined which domain(s) of FAK is(are) important for various vascular functions such as FA recruiting, XIAP-binding and shear stress-stimulated ERK activation. Through a series of experiments, we determined that the FRNK domain is recruited into FA sites and promotes endothelial cell adhesion. Interestingly, XIAP knockdown was shown to reduce FA recruitment of FRNK and the cell adhesive effect of FRNK. In addition, we found that XIAP interacts with FRNK, suggesting cross-talk between XIAP and FRNK. We also demonstrated that FRNK inhibits endothelial cell migration and shear-stimulated ERK activation. These inhibitory effects of FRNK were reversed by XIAP knockdown. Taken together, we can conclude that XIAP plays a key role in vascular functions of FRNK or FRNK domain-mediated vascular functions of FAK.