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 (-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.

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