The ezrin protein family: membrane-cytoskeleton interactions and disease associations
A Vaheri, O Carpén, L Heiska, TS Helander… - Current opinion in cell …, 1997 - Elsevier
A Vaheri, O Carpén, L Heiska, TS Helander, J Jääskeläinen, P Majander-Nordenswan…
Current opinion in cell biology, 1997•ElsevierEzrin, radixin, moesin and merlin form a subfamily of conserved proteins in the band 4.1
superfamily. Ezrin protein subfamily members act as linkers between the plasma membrane
and the cytoskeleton. Members of the subfamily have been shown to interact with each
other, with cell adhesion molecules such as CD44 and with F-actin. Recent data indicate
that intercellular adhesion molecules 1 and 2 also interact with ezrin. The proteins are also
involved in the redistribution of intercellular adhesion molecules and the organization of cell …
superfamily. Ezrin protein subfamily members act as linkers between the plasma membrane
and the cytoskeleton. Members of the subfamily have been shown to interact with each
other, with cell adhesion molecules such as CD44 and with F-actin. Recent data indicate
that intercellular adhesion molecules 1 and 2 also interact with ezrin. The proteins are also
involved in the redistribution of intercellular adhesion molecules and the organization of cell …
Ezrin, radixin, moesin and merlin form a subfamily of conserved proteins in the band 4.1 superfamily. Ezrin protein subfamily members act as linkers between the plasma membrane and the cytoskeleton. Members of the subfamily have been shown to interact with each other, with cell adhesion molecules such as CD44 and with F-actin. Recent data indicate that intercellular adhesion molecules 1 and 2 also interact with ezrin. The proteins are also involved in the redistribution of intercellular adhesion molecules and the organization of cell membrane structures. Merlin is a tumor suppressor that is involved in tumorigenesis of schwannomas and meningiomas. Merlin has the same overall protein structure as the other proteins in the subfamily but may have partially distinct functions.
Elsevier