CLIC proteins, ezrin, radixin, moesin and the coupling of membranes to the actin cytoskeleton

A smoking gun?

Lele Jiang, Juanita M. Phang, Jiang Yu, Stephen J. Harrop, Anna V. Sokolova, Anthony P. Duff, Krystyna E. Wilk, Heba Alkhamici, Samuel N. Breit, Stella M. Valenzuela, Louise J. Brown, Paul M G Curmi*

*Corresponding author for this work

Research output: Contribution to journalArticle

37 Citations (Scopus)


The CLIC proteins are a highly conserved family of metazoan proteins with the unusual ability to adopt both soluble and integral membrane forms. The physiological functions of CLIC proteins may include enzymatic activity in the soluble form and anion channel activity in the integral membrane form. CLIC proteins are associated with the ERM proteins: ezrin, radixin and moesin. ERM proteins act as cross-linkers between membranes and the cortical actin cytoskeleton. Both CLIC and ERM proteins are controlled by Rho family small GTPases. CLIC proteins, ERM and Rho GTPases act in a concerted manner to control active membrane processes including the maintenance of microvillar structures, phagocytosis and vesicle trafficking. All of these processes involve the interaction of membranes with the underlying cortical actin cytoskeleton. The relationships between Rho GTPases, CLIC proteins, ERM proteins and the membrane:actin cytoskeleton interface are reviewed. Speculative models are proposed involving the formation of localised multi-protein complexes on the membrane surface that assemble via multiple weak interactions. This article is part of a Special Issue entitled: Reciprocal influences between cell cytoskeleton and membrane channels, receptors and transporters. Guest Editor: Jean Claude Hervé.

Original languageEnglish
Pages (from-to)643-657
Number of pages15
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number2
Publication statusPublished - Feb 2014


  • Actin cytoskeleton
  • CLIC
  • Ezrin, radixin, moesin
  • Membrane remodeling
  • Rho GTPase
  • Vesicle trafficking

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