ERM proteins in cell adhesion and membrane dynamics

被引:325
作者
Mangeat, P [1 ]
Roy, C [1 ]
Martin, M [1 ]
机构
[1] Univ Montpellier 2, CNRS UMR 5539, F-34095 Montpellier 05, France
关键词
D O I
10.1016/S0962-8924(99)01544-5
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Ezrin, radixin and moesin, collectively known as the ERM proteins, are a group of closely related mernbrane-cytoskeleton linkers that regulate cell adhesion and cortical morphogenesis. ERM proteins can self-associate through intra- and inter-molecular interactions, and these interactions mask several binding sites on the proteins. ERM activation involves unfolding of the molecule, and allows the protein to bind to plasma membrane components either directly, or indirectly through linker proteins. The discovery that the tumour-suppressor NF2, also known as merlin/schwannomin, is related to ERM proteins has added a new impetus to investigations of their roles. This review discusses current understanding of the structure and function of members of the ERM family of proteins.
引用
收藏
页码:187 / 192
页数:6
相关论文
共 59 条
  • [21] Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization
    LaJeunesse, DR
    McCartney, BM
    Fehon, RG
    [J]. JOURNAL OF CELL BIOLOGY, 1998, 141 (07) : 1589 - 1599
  • [22] Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts
    Lamb, RF
    Ozanne, BW
    Roy, C
    McGarry, L
    Stipp, C
    Mangeat, P
    Jay, DG
    [J]. CURRENT BIOLOGY, 1997, 7 (09) : 682 - 688
  • [23] The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3
    Lamprecht, G
    Weinman, EJ
    Yun, CHC
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (45) : 29972 - 29978
  • [24] Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44
    Legg, JW
    Isacke, CM
    [J]. CURRENT BIOLOGY, 1998, 8 (12) : 705 - 708
  • [25] Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    Mackay, DJG
    Esch, F
    Furthmayr, H
    Hall, A
    [J]. JOURNAL OF CELL BIOLOGY, 1997, 138 (04) : 927 - 938
  • [26] EZRIN NH2-TERMINAL DOMAIN INHIBITS THE CELL EXTENSION ACTIVITY OF THE COOH-TERMINAL DOMAIN
    MARTIN, M
    ANDREOLI, C
    SAHUQUET, A
    MONTCOURRIER, P
    ALGRAIN, M
    MANGEAT, P
    [J]. JOURNAL OF CELL BIOLOGY, 1995, 128 (06) : 1081 - 1093
  • [27] Three determinants in ezrin are responsible for cell extension activity
    Martin, M
    Roy, C
    Montcourrier, P
    Sahuquet, A
    Mangeat, P
    [J]. MOLECULAR BIOLOGY OF THE CELL, 1997, 8 (08) : 1543 - 1557
  • [28] Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    Matsui, T
    Maeda, M
    Doi, Y
    Yonemura, S
    Amano, M
    Kaibuchi, K
    Tsukita, S
    Tsukita, S
    [J]. JOURNAL OF CELL BIOLOGY, 1998, 140 (03) : 647 - 657
  • [29] The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation
    McClatchey, AI
    Saotome, I
    Ramesh, V
    Gusella, JF
    Jacks, T
    [J]. GENES & DEVELOPMENT, 1997, 11 (10) : 1253 - 1265
  • [30] NHE-RF, a regulatory cofactor for Na+-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins
    Murthy, A
    Gonzalez-Agosti, C
    Cordero, E
    Pinney, D
    Candia, C
    Solomon, F
    Gusella, J
    Ramesh, V
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (03) : 1273 - 1276