Phosphatidylinositol 4,5-bisphosphate-induced conformational change of ezrin and formation of ezrin oligomers.
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. PIP₂ 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.
Carvalho
Kevin
K
Laboratoire des Colloïdes, Verres et Nanomatériaux, UMR CNRS-UM2 no. 5587, Université Montpellier 2, Place E. Bataillon, Montpellier Cedex 5, France.
Khalifat
Nada
N
Maniti
Ofelia
O
Nicolas
Claire
C
Arold
Stefan
S
Picart
Catherine
C
Ramos
Laurence
L
D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000378:metabolism*; D003599:Cytoskeleton; D006801:Humans; D008565:Membrane Proteins; D050505:Mutant Proteins; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism*; D011487:Protein Conformation; D055503:Protein Multimerization; D000099149:Ezrin
D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D050505:Mutant Proteins; D019269:Phosphatidylinositol 4,5-Diphosphate; D000099149:Ezrin