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

Yosuke Senju, Emi Hibino

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Article number184076
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1865
Issue number2
DOIs
Publication statusPublished - Feb 2023

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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