(Downloading may take up to 30 seconds.
If the slide opens in your browser, select File -> Save As to save it.)

Click on image to view larger version.



Fig. 9. Effects of disrupting {alpha}-actinin localization on focal adhesion dynamics. (A) Still images from video sequences of CHOK1 cells co-transfected with RFP-zyxin and full-length GFP—{alpha}-actinin (a), {alpha}-actinin-head—GFP (b) or {alpha}-actinin-rod—GFP (c) (Movies 12, 13 and 14, respectively) RFP-zyxin-containing focal complexes are more peripheral and less dynamic when {alpha}-actinin localization to the focal complex is disrupted by {alpha}-actinin-rod—GFP, similar to calpain inhibition. In contrast, RFP-zyxin in {alpha}-actinin-head—GFP co-transfected cells exhibits a focal adhesion distribution and dynamics similar to full-length GFP—{alpha}-actinin (Movies 11-13). Bar, 20 µm. (B) Quantification of focal adhesion dynamics in cells co-transfected with full-length {alpha}-actinin, {alpha}-actinin-head—GFP, or {alpha}-actinin-rod—GFP and RFP-zyxin. Transfection of {alpha}-actinin-rod—GFP inhibits focal adhesion disassembly when compared with full-length {alpha}-actinin (P<0.002) and with {alpha}-actinin-head—GFP (P<0.003). Quantification of focal adhesion dynamics was performed on five cells for each condition.