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
  • [1] Amieva MR, 1999, J CELL SCI, V112, P111
  • [2] EZRIN OLIGOMERS ARE MAJOR CYTOSKELETAL COMPONENTS OF PLACENTAL MICROVILLI - A PROPOSAL FOR THEIR INVOLVEMENT IN CORTICAL MORPHOGENESIS
    BERRYMAN, M
    GARY, R
    BRETSCHER, A
    [J]. JOURNAL OF CELL BIOLOGY, 1995, 131 (05) : 1231 - 1242
  • [3] Bretscher A, 1997, J CELL SCI, V110, P3011
  • [4] DEPHOSPHORYLATION OF EZRIN AS AN EARLY EVENT IN RENAL MICROVILLAR BREAKDOWN AND ANOXIC INJURY
    CHEN, J
    COHN, JA
    MANDEL, LJ
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (16) : 7495 - 7499
  • [5] The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane
    Chishti, AH
    Kim, AC
    Marfatia, SM
    Lutchman, M
    Hanspal, M
    Jindal, H
    Liu, SC
    Low, PS
    Rouleau, GA
    Mohandas, N
    Chasis, JA
    Conboy, JG
    Gascard, P
    Takakuwa, Y
    Huang, SC
    Benz, EJ
    Bretscher, A
    Fehon, RG
    Gusella, AF
    Ramesh, V
    Solomon, F
    Marchesi, VT
    Tsukita, S
    Tsukita, S
    Arpin, M
    Louvard, D
    Tonks, NK
    Anderson, JM
    Fanning, AS
    Bryant, PJ
    Woods, DF
    Hoover, KB
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (08) : 281 - 282
  • [6] Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
    Crepaldi, T
    Gautreau, A
    Comoglio, PM
    Louvard, D
    Arpin, M
    [J]. JOURNAL OF CELL BIOLOGY, 1997, 138 (02) : 423 - 434
  • [7] Normal development of mice and unimpaired cell adhesion cell motility actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout
    Doi, Y
    Itoh, M
    Yonemura, S
    Ishihara, S
    Takano, H
    Noda, T
    Tsukita, S
    Tsukita, S
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (04) : 2315 - 2321
  • [8] Ezrin is a cyclic AMP-dependent protein kinase anchoring protein
    Dransfield, DT
    Bradford, AJ
    Smith, J
    Martin, M
    Roy, C
    Mangeat, PH
    Goldenring, JR
    [J]. EMBO JOURNAL, 1997, 16 (01) : 35 - 43
  • [9] Association of the myosin-binding subunit of myosin phosphatase and moesin: Dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase
    Fukata, Y
    Kimura, K
    Oshiro, N
    Saya, H
    Matsuura, Y
    Kaibuchi, K
    [J]. JOURNAL OF CELL BIOLOGY, 1998, 141 (02) : 409 - 418
  • [10] EZRIN SELF-ASSOCIATION INVOLVES BINDING OF AN N-TERMINAL DOMAIN TO A NORMALLY MASKED C-TERMINAL DOMAIN THAT INCLUDES THE F-ACTIN BINDING-SITE
    GARY, R
    BRETSCHER, A
    [J]. MOLECULAR BIOLOGY OF THE CELL, 1995, 6 (08) : 1061 - 1075