RNAi knockdown of the focal adhesion protein TES reveals its role in actin stress fibre organisation
Article first published online: 20 JAN 2005
Copyright © 2005 Wiley-Liss, Inc.
Cell Motility and the Cytoskeleton
Volume 60, Issue 3, pages 140–152, March 2005
How to Cite
Griffith, E., Coutts, A. S. and Black, D. M. (2005), RNAi knockdown of the focal adhesion protein TES reveals its role in actin stress fibre organisation. Cell Motil. Cytoskeleton, 60: 140–152. doi: 10.1002/cm.20052
- Issue published online: 14 FEB 2005
- Article first published online: 20 JAN 2005
- Manuscript Accepted: 9 NOV 2004
- Manuscript Received: 7 JUL 2004
- Cancer Research UK
- focal adhesion;
- actin stress fibres
TES was originally identified as a candidate tumour suppressor gene and has subsequently been found to encode a novel focal adhesion protein. As well as localising to cell-matrix adhesions, TES localises to cell-cell contacts and to actin stress fibres. TES interacts with a variety of cytoskeletal proteins including zyxin, mena, VASP, talin and actin. There is evidence that TES may function in actin-dependent processes as overexpression of TES results in increased cell spreading and decreased cell motility. Together with TES's interacting partners, these data suggest that TES might be involved in regulation of the actin cytoskeleton. Here, for the first time, we have used RNAi to successfully knockdown TES in HeLa cells and we demonstrate that loss of TES from focal adhesions results in loss of actin stress fibres. Similarly, and as previously reported, RNAi-mediated knockdown of zyxin results in loss of actin stress fibres. TES siRNA treated cells show reduced RhoA activity, suggesting that the Rho GTPase pathway may be involved in the TES RNAi-induced loss of stress fibres. We have also used RNAi to examine the requirement of TES and zyxin for each other's localisation at focal adhesions, and we propose a hierarchy of recruitment, with zyxin being first, followed by VASP and then TES. Cell Motil. Cytoskeleton 60:140–152, 2005. © 2005 Wiley-Liss, Inc.