Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 419-424 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 419 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2012 Mar 9 |
Fingerprint
Keywords
- Endothelial cells
- FAK
- Focal adhesions
- FRNK
- XIAP
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
Cite this
XIAP reverses various functional activities of FRNK in endothelial cells. / Ahn, Sunyoung; Kim, Hyun Jeong; Chi, Sung-Gil; Park, Heonyong.
In: Biochemical and Biophysical Research Communications, Vol. 419, No. 2, 09.03.2012, p. 419-424.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - XIAP reverses various functional activities of FRNK in endothelial cells
AU - Ahn, Sunyoung
AU - Kim, Hyun Jeong
AU - Chi, Sung-Gil
AU - Park, Heonyong
PY - 2012/3/9
Y1 - 2012/3/9
N2 - 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.
AB - 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.
KW - Endothelial cells
KW - FAK
KW - Focal adhesions
KW - FRNK
KW - XIAP
UR - http://www.scopus.com/inward/record.url?scp=84862829624&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84862829624&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2012.02.037
DO - 10.1016/j.bbrc.2012.02.037
M3 - Article
C2 - 22366087
AN - SCOPUS:84862829624
VL - 419
SP - 419
EP - 424
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 2
ER -