Binding Partners
TES does not appear to be an enzyme; rather it is a protein that mediates/regulates cellular functions via Protein:protein interactions. Pull down experiments reveal that TES has putative interactions mediated by the indicated domain:
| Partner | Domain | ref | Method |
|---|---|---|---|
| mENA/VASP | LIM3 | Yeast two Hybrid, Pull-down assay, Structure, ITC | |
| Arp7a | ??? | Yeast two Hybrid | |
| Zyxin | LIM1 | Yeast two Hybrid, Pull-down assay | |
| Actin | PET? | Pull-down assay | |
| α-Actinin | PET? | Pull-down assay | |
| Paxillin | PET? | Pull-down assay |
Garvalov et al. showed that the interaction between TES & zyxin were direct, using recombinant proteins expressed in E. coli.
Some of the potential binding partners (Zyxin, mENA) can be found in focal adhesion complexes; the range of binding partners indicates a potential role for TES in-between 'privileged' Actin polymerisation and focal adhesion contacts to the extracellular matrix. This tallies with the observation that GFP-tagged TES can be seen at focal adhesions.
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