(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. 2. Merlin structure and interactions. (A) Merlin contains three conserved protein-protein interaction domains: a FERM domain in its N-terminus and a C-terminal domain (CTD) separated by a coiled-coil ({alpha}-helical) region. Crystallography showed that the merlin FERM domain contains three subdomains, which exhibits a cloverleaf architecture. Merlin FERM has a unique `Blue Box' (BB, residues 177-183) compared with other ERM proteins. (B) Merlin can adopt two conformations: a `closed' active and `open' inactive form. Merlin can switch from these two conformations as a result of phosphorylation, lipid binding, protein interactions or NF2 mutations. (C) Merlin interacts with several molecules, including NHE-RF, ßII-spectrin, CD44, other ERM proteins, SCHIP-1, HRS, actin and syntenin, which may affect merlin function as a growth suppressor. The proposed domains in merlin that mediate these interactions are depicted.