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Moesin-ezrin-radixin-like protein merlin: Its conserved and distinct functions from those of ERM proteins

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DOI: 10.1016/j.bbamem.2022.184076

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Merlin (moesin-ezrin-radixin-like protein); Phosphatidylinositol 45-bisphosphate (PI(4,5)P-2); Ezrin-radixin-moesin (ERM); Cell-cell adhesions; Contact inhibition of proliferation; Epithelial-mesenchymal transition (EMT)

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Neurofibromatosis type 2 (NF2), caused by the mutated merlin gene, belongs to the FERM domain-containing 4.1 superfamily. Merlin, a tumor suppressor, shares sequence homology with ERM proteins and plays important roles in cell-cell adhesions. This article provides insights into the molecular functions of merlin and its interactions with PI(4,5)P2, shedding light on its fundamental roles in cells and tissues.
Neurofibromatosis type 2 (NF2), which encodes merlin (moesin-ezrin-radixin-like protein), belongs to the band 4.1, ezrin, radixin, moesin (FERM) domain-containing 4.1 superfamily. Merlin shares sequence homology with ERM proteins, is evolutionarily conserved, and acts as a tumour suppressor. Here, we describe the molecular functions of merlin from a biophysical point of view. We describe the structural basis for merlin regulatory mechanisms based on its interaction with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) along with its interaction partners, and then describe its physiological functions in cell-cell adhesions. Elucidation of these merlin functions will lead to a clear understanding of its fundamental roles in cells and tissues.

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