作者: Jin-Jun Meng , D.J. Lowrie , Hao Sun , Emily Dorsey , Patricia D. Pelton
DOI: 10.1002/1097-4547(20001115)62:4<491::AID-JNR3>3.0.CO;2-D
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摘要: The product of the neurofibromatosis type II (NF2) tumor suppressor gene, merlin, is closely related to ezrin-radixin-moesin (ERM) family, a group proteins believed link cytoskeleton plasma membrane. Mutation in NF2 locus associated with Schwann cell tumors (schwannomas). two predominant merlin isoforms, I and II, differ only carboxy-terminal 16 residues isoform anti-proliferative. Merlin lacks an actin-binding domain conserved among ezrin, radixin moesin. Because ezrin moesin are co-expressed cells, all homodimerize, we have examined whether dimerize one another. We found by immunoprecipitation yeast two-hybrid assays that both isoforms interact ezrin. interaction occurs head-to-tail orientation, amino-terminal half protein interacting other. behave differently their Isoform binds whose carboxy-terminus exposed, whereas regardless open or closed conformation. heterodimerization much stronger than between either can inhibit merlin-ezrin binding. This suggests that, vivo, dimerization could regulate merlin-ERM interaction, thus indirectly other interactions involving ERM proteins. J. Neurosci. Res. 62:491–502, 2000. © 2000 Wiley-Liss, Inc.