The ezrin protein family: membrane-cytoskeleton interactions and disease associations

被引：173

作者：

Vaheri, A

Carpen, O

Heiska, L

Helander, TS

Jaaskelainen, J

MajanderNordenswan, P

Sainio, M

Timonen, T

Turunen, O

机构：

[1] Haartman Institute, University of Helsinki, FIN-00014 Helsinki

来源：

CURRENT OPINION IN CELL BIOLOGY | 1997年 / 9卷 / 05期

关键词：

D O I：

10.1016/S0955-0674(97)80119-6

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：659 / 666

页数：8

共 70 条

[41] IDENTIFICATION OF A PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE-BINDING DOMAIN IN THE N-TERMINAL REGION OF EZRIN [J].