biostudies-literatureUnknown302(1)Ackermann ELMGerman Research FoundationBMBF BonnEzrin, a member of the ezrin, radixin, moesin (ERM) protein family, is a critical and ancient protein responsible for actin binding and organization. It anchors to the plasma membrane via its FERM domain and interfaces with the actin cortex through its C-terminal filamentous actin (F-actin)-binding domain (C-terminal ERM association domain [C-ERMAD]), thereby regulating actin dynamics in processes such as phagocytosis, microvillus formation, and tumor cell metastasis. Although ezrin's interactions with plasma membrane receptors have been extensively characterized and are therefore well understood, the molecular details of the ezrin-F-actin interaction remain largely unexplored. To address this knowledge gap, we employed minimal actin cortices based on planar supported lipid bilayers, to whThe Journal of biological chemistry111031https://www.ebi.ac.uk/biostudies/studies/S-EPMC12796735biostudies-literatureMinimal actin cortices: The αD-helix of ezrin's C-ERMAD governs F-actin binding.PMC12796735Ackermann ELMHeißenberg TSteinem CRathke JfalseMinimal actin cortices: The αD-helix of ezrin's C-ERMAD governs F-actin binding.Ezrin, a member of the ezrin, radixin, moesin (ERM) protein family, is a critical and ancient protein responsible for actin binding and organization. It anchors to the plasma membrane via its FERM domain and interfaces with the actin cortex through its C-terminal filamentous actin (F-actin)-binding domain (C-terminal ERM association domain [C-ERMAD]), thereby regulating actin dynamics in processes such as phagocytosis, microvillus formation, and tumor cell metastasis. Although ezrin's interactions with plasma membrane receptors have been extensively characterized and are therefore well understood, the molecular details of the ezrin-F-actin interaction remain largely unexplored. To address this knowledge gap, we employed minimal actin cortices based on planar supported lipid bilayers, to wh2025-01-01T00:00:00Z2025 Dec2026-06-06T15:18:09.947Z2026-06-01T03:10:47.896ZS-EPMC127967354138097110.1016/j.jbc.2025.111031