» Articles » PMID: 21343695

Emerging Role for ERM Proteins in Cell Adhesion and Migration

Overview
Journal Cell Adh Migr
Specialty Cell Biology
Date 2011 Feb 24
PMID 21343695
Citations 118
Authors
Affiliations
Soon will be listed here.
Abstract

The highly related ERM (Ezrin, Radixin, Moesin) proteins provide a regulated linkage between the membrane and the underlying actin cytoskeleton. They also provide a platform for the transmission of signals in responses to extracellular cues. Studies in different model organisms and in cultured cells have highlighted the importance of ERM proteins in the generation and maintenance of specific domains of the plasma membrane. A central question is how do ERM proteins coordinate actin filament organization and membrane protein transport/stability with signal transduction pathways to build up complex structures? Through their interaction with numerous partners including membrane proteins, actin cytoskeleton and signaling molecules, ERM proteins have the ability to organize multiprotein complexes in specific cellular compartments. Likewise, ERM proteins participate in diverse functions including cell morphogenesis, endocytosis/exocytosis, adhesion and migration. This review focuses on aspects still poorly understood related to the function of ERM proteins in epithelial cell adhesion and migration.

Citing Articles

Moesin contributes to heat shock gene response through direct binding to the Med15 subunit of the Mediator complex in the nucleus.

Kristo I, Kovacs Z, Szabo A, Borkuti P, Graf A, Santa A Open Biol. 2024; 14(10):240110.

PMID: 39353569 PMC: 11444770. DOI: 10.1098/rsob.240110.


VEGFD signaling balances stability and activity-dependent structural plasticity of dendrites.

Aksan B, Kenkel A, Yan J, Sanchez Romero J, Missirlis D, Mauceri D Cell Mol Life Sci. 2024; 81(1):354.

PMID: 39158743 PMC: 11335284. DOI: 10.1007/s00018-024-05357-2.


Ezrin, radixin, and moesin are dispensable for macrophage migration and cellular cortex mechanics.

Verdys P, Rey Barroso J, Girel A, Vermeil J, Bergert M, Sanchez T EMBO J. 2024; 43(21):4822-4845.

PMID: 39026000 PMC: 11535515. DOI: 10.1038/s44318-024-00173-7.


The Expression of Rab8, Ezrin, Radixin and Moesin in the Ciliary Body of Cynomolgus Monkeys.

Tanabe K, Kimura I, Okamoto H, Chi Z, Akahori M, Shimozawa N Juntendo Iji Zasshi. 2024; 68(4):339-351.

PMID: 39021423 PMC: 11250011. DOI: 10.14789/jmj.JMJ21-0042-OA.


MicroRNA-409: Molecular functions and clinical applications in cancer.

Rajabloo Y, Latifi H, Akhlaghipour I, Taghehchian N, Moghbeli M Biochem Biophys Rep. 2024; 38:101728.

PMID: 38737729 PMC: 11087923. DOI: 10.1016/j.bbrep.2024.101728.


References
1.
Legg J, Isacke C . Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44. Curr Biol. 1998; 8(12):705-8. DOI: 10.1016/s0960-9822(98)70277-5. View

2.
Elliott B, Meens J, SenGupta S, Louvard D, Arpin M . The membrane cytoskeletal crosslinker ezrin is required for metastasis of breast carcinoma cells. Breast Cancer Res. 2005; 7(3):R365-73. PMC: 1143558. DOI: 10.1186/bcr1006. View

3.
Kikuchi S, Hata M, Fukumoto K, Yamane Y, Matsui T, Tamura A . Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Nat Genet. 2002; 31(3):320-5. DOI: 10.1038/ng905. View

4.
Akhtar N, Hotchin N . RAC1 regulates adherens junctions through endocytosis of E-cadherin. Mol Biol Cell. 2001; 12(4):847-62. PMC: 32271. DOI: 10.1091/mbc.12.4.847. View

5.
Reczek D, Berryman M, BRETSCHER A . Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J Cell Biol. 1997; 139(1):169-79. PMC: 2139813. DOI: 10.1083/jcb.139.1.169. View