Structural highlights
Function
[TES_HUMAN] Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The intracellular targeting of Ena/VASP family members is achieved via the interaction of their EVH1 domain with FPPPP sequence motifs found in a variety of cytoskeletal proteins, including lamellipodin, vinculin, and zyxin. Here we show that the LIM3 domain of Tes, which lacks the FPPPP motif, binds to the EVH1 domain of Mena, but not to those of VASP or Evl. The structure of the LIM3:EVH1 complex reveals that Tes occludes the FPPPP-binding site and competes with FPPPP-containing proteins for EVH1 binding. Structure-based gain-of-function experiments define the molecular basis for the specificity of the Tes-Mena interaction. Consistent with in vitro observations, the LIM3 domain displaces Mena, but not VASP, from the leading edge and focal adhesions. It also regulates cell migration through a Mena-dependent mechanism. Our observations identify Tes as an atypical EVH1 binding partner and a regulator specific to a single Ena/VASP family member.
Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding.,Boeda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M Mol Cell. 2007 Dec 28;28(6):1071-82. PMID:18158903[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tobias ES, Hurlstone AF, MacKenzie E, McFarlane R, Black DM. The TES gene at 7q31.1 is methylated in tumours and encodes a novel growth-suppressing LIM domain protein. Oncogene. 2001 May 17;20(22):2844-53. PMID:11420696 doi:http://dx.doi.org/10.1038/sj.onc.1204433
- ↑ Garvalov BK, Higgins TE, Sutherland JD, Zettl M, Scaplehorn N, Kocher T, Piddini E, Griffiths G, Way M. The conformational state of Tes regulates its zyxin-dependent recruitment to focal adhesions. J Cell Biol. 2003 Apr 14;161(1):33-9. PMID:12695497 doi:http://dx.doi.org/10.1083/jcb.200211015
- ↑ Coutts AS, MacKenzie E, Griffith E, Black DM. TES is a novel focal adhesion protein with a role in cell spreading. J Cell Sci. 2003 Mar 1;116(Pt 5):897-906. PMID:12571287
- ↑ Boeda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M. Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding. Mol Cell. 2007 Dec 28;28(6):1071-82. PMID:18158903 doi:10.1016/j.molcel.2007.10.033
