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Published online December 26, 2006
doi:10.1083/jcb.200608015
The Journal of Cell Biology, Vol. 176, No. 1, 43-49
The Rockefeller University Press, 0021-9525 $30.00
© 2006 Liao et al.
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 The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1

Yi-Chun Liao1,2, Lizhen Si1,2, Ralph W. deVere White3, and Su Hao Lo1,2

1 Center for Tissue Regeneration and Repair, 2 Department of Orthopedic Surgery, and 3 Department of Urology, University of California, Davis, Sacramento, CA 95817

Correspondence to Su Hao Lo: shlo{at}ucdavis.edu

The tensin family member cten (C-terminal tensin like) is an Src homology 2 (SH2) and phosphotyrosine binding domain–containing focal adhesion molecule that may function as a tumor suppressor. However, the mechanism has not been well established. We report that cten binds to another tumor suppressor, deleted in liver cancer 1 (DLC-1), and the SH2 domain of cten is responsible for the interaction. Unexpectedly, the interaction between DLC-1 and the cten SH2 domain is independent of tyrosine phosphorylation of DLC-1. By site-directed mutagenesis, we have identified several amino acid residues on cten and DLC-1 that are essential for this interaction. Mutations on DLC-1 perturb the interaction with cten and disrupt the focal adhesion localization of DLC-1. Furthermore, these DLC-1 mutants have lost their tumor suppression activities. When these DLC-1 mutants were fused to a focal adhesion targeting sequence, their tumor suppression activities were significantly restored. These results provide a novel mechanism whereby the SH2 domain of cten-mediated focal adhesion localization of DLC-1 plays an essential role in its tumor suppression activity.

Abbreviations used in this paper: cten, C-terminal tensin like; DLC-1, deleted in liver cancer 1; FAB, focal adhesion binding; PTB, phosphotyrosine binding; RhoGAP, RhoGTPase-activating protein; SAM, sterile {alpha} motif; SH2, Src homology 2; START, steroidogenic acute regulatory-related lipid transfer.


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