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The ERM protein family consists of three closely related proteins, ezrin, radixin and moesin. The three paralogs, ezrin, radixin and moesin, are present in vertebrates, whereas other species have only one ERM gene. Therefore, in vertebrates these paralogs likely arose by gene duplication. ERM proteins are highly conserved throughout evolution. More than 75% identity is observed in the N-terminal and the C-terminal of vertebrates (ezrin, radixin, moesin), ''Drosophila'' (dmoesin) and ''C. elegans'' (ERM-1) homologs. ==Structure== ERM molecules contain the following three domains:〔 * N-terminal globular domain, also called FERM domain (Band 4.1, ezrin, radixin, moesin). The FERM domain allows ERM proteins to interact with integral proteins of the plasma membrane, or scaffolding proteins localized beneath the plasma membrane.〔 The FERM domain is composed of three subdomains (F1, F2, F3) that are arranged as a cloverleaf. * extended alpha-helical domain. * charged C-terminal domain. This domain mediates the interaction with F-actin. Ezrin, radixin and merlin also contain a polyproline region between the central helical and C-terminal domains. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「ERM protein family」の詳細全文を読む スポンサード リンク
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