Phosphatidylinositol 4,5-bisphosphate-induced conformational change of ezrin and formation of ezrin oligomers

Kevin Carvalho, Nada Khalifat, Ofelia Maniti, Claire Nicolas, Stefan Arold, Catherine Picart*, Laurence Ramos

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The plasma membrane-cytoskeleton interface is a dynamic structure involved in a variety of cellular events. Ezrin, a protein from the ERM family, provides a direct linkage between the cytoskeleton and the membrane via its interaction with phosphatidylinositol 4,5-bisphosphate (PIP2). In this paper, we investigate the interaction between PIP2 and ezrin in vitro using PIP2 dispersed in a unimolecular way in buffer. We compared the results obtained with full-length ezrin to those obtained with an ezrin mutant, which was previously found not to be localized at the cell membrane, and with the N-terminal membrane binding domain (FERM domain) of ezrin. We show that PIP2 induced a conformational change in full-length ezrin. PIP 2 was also found to induce, in vitro, the formation of oligomers of wild-type ezrin, but not of mutant ezrin. These oligomers had previously been observed in vivo, but their role is yet to be clarified. Our finding hints at a possible role for PIP2 in the formation of ezrin oligomers.

Original languageEnglish (US)
Pages (from-to)9318-9327
Number of pages10
JournalBiochemistry
Volume49
Issue number43
DOIs
StatePublished - Nov 2 2010

ASJC Scopus subject areas

  • Biochemistry

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