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Updated: Mar 30, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

M A Pearson1, D Reczek, A Bretscher

  • 1Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.

Cell
|June 10, 2000
PubMed

Insights

The ezrin-radixin-moesin (ERM) protein family regulates cell structure. Their dormant state reveals a novel activation mechanism involving FERM and tail domain interactions, offering insights into cell signaling and merlin regulation.

Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Structural Biology

Background:

  • The ezrin-radixin-moesin (ERM) protein family acts as a crucial link between actin filaments and the plasma membrane.
  • ERM proteins possess an N-terminal FERM domain for membrane binding and a C-terminal F-actin binding site.
  • Regulation occurs via an intramolecular interaction masking these binding sites.

Purpose of the Study:

  • To elucidate the structural basis of ERM protein dormancy.
  • To understand the novel mechanism of ERM protein activation.
  • To explore potential similarities in regulation with the tumor suppressor merlin.

Main Methods:

  • X-ray crystallography to determine the structure of a dormant moesin FERM/tail complex.

Main Results:

  • The crystal structure revealed a dormant moesin FERM/tail complex with a three-lobed FERM domain.
  • The C-terminal segment was bound as an extended peptide, masking a significant portion of the FERM domain surface.
  • This binding mode suggests a new pathway for signal-induced activation.

Conclusions:

  • The FERM/tail complex structure provides a molecular understanding of ERM protein dormancy.
  • The findings propose a novel mechanism for ERM protein activation by external signals.
  • Sequence conservation implies similar regulatory mechanisms for the tumor suppressor merlin.

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