| First Author | Terawaki S | Year | 2006 |
| Journal | Structure | Volume | 14 |
| Issue | 4 | Pages | 777-89 |
| PubMed ID | 16615918 | Mgi Jnum | J:247408 |
| Mgi Id | MGI:5926357 | Doi | 10.1016/j.str.2006.01.015 |
| Citation | Terawaki S, et al. (2006) Structural basis for NHERF recognition by ERM proteins. Structure 14(4):777-89 |
| abstractText | The Na+/H+ exchanger regulatory factor (NHERF) is a key adaptor protein involved in the anchoring of ion channels and receptors to the actin cytoskeleton through binding to ERM (ezrin/radixin/moesin) proteins. NHERF binds the FERM domain of ERM proteins, although NHERF has no signature Motif-1 sequence for FERM binding found in adhesion molecules. The crystal structures of the radixin FERM domain complexed with the NHERF-1 and NHERF-2 C-terminal peptides revealed a peptide binding site of the FERM domain specific for the 13 residue motif MDWxxxxx(L/I)Fxx(L/F) (Motif-2), which is distinct from Motif-1. This Motif-2 forms an amphipathic alpha helix for hydrophobic docking to subdomain C of the FERM domain. This docking causes induced-fit conformational changes in subdomain C and affects binding to adhesion molecule peptides, while the two binding sites are not overlapped. Our studies provide structural paradigms for versatile ERM linkages between membrane proteins and the cytoskeleton. |
