ERM proteins and merlin: Integrators at the cell cortex

Nature Reviews Molecular Cell Biology

Volumn 3, Issue 8, 2002, Pages 586-599

  Bretscher, Anthony ^a   Edwards, Kevin ^b   Fehon, Richard G ^c  

^a Cornell University ^*  (United States)

^b ILLINOIS STATE UNIVERSITY   (United States)

^c DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EZRIN; MEMBRANE PROTEIN; MERLIN; MOESIN; RADIXIN;

BRAIN CELL; BRAIN CORTEX; CELL MEMBRANE; CELL SHAPE; CYTOSKELETON; ENDOCYTOSIS; EXOCYTOSIS; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; REGULATORY MECHANISM; REVIEW;

ANIMALS; BLOOD PROTEINS; CELL LINE; CELL MEMBRANE; CELL POLARITY; CYTOSKELETAL PROTEINS; CYTOSKELETON; HUMANS; MEMBRANE PROTEINS; MICROFILAMENT PROTEINS; MODELS, BIOLOGICAL; MULTIGENE FAMILY; NEUROFIBROMIN 2; PHOSPHOPROTEINS; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; TUMOR SUPPRESSOR PROTEINS;

FALCO COLUMBARIUS;

EID: 0036346708     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm882     Document Type: Review

References (139)

1. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
2. Purification of an 80, 000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells
3. r 75, 000 plasma membrane protein of human choriocarcinoma cells
4. The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein
5. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
6. A new 82-kD barbed endcapping protein (radixin) localized in the cell-to-cell adherens junction: Purification and characterization
7. Redixin is a component of hepatocyte microvilli in situ
8. A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation
9. Cdna cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1
10. Moesin: A member of the protein 4.1-talin-ezrin family of proteins
11. Radixin is a novel member of the band 4.1 family
12. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor
13. Alteration in a new gene encoding a putative membrane-organizing protein causes neurofibromatosis type 2
14. Merlin: The neurofibromatosis 2 tumor suppressor
15. ERMmerlin and EBP50 protein families in plasma membrane organization and function
16. ERM proteins in cell adhesion and membrane dynamics
17. Cortical actin organization: Lessons from ERM (ezrin/radixin/moesin) proteins
18. 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
19. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members
20. ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse
21. Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus
22. Ezrin is an effector of hepatocyte growth factormediated migration and morphogenesis in epithelial cells
23. The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation
24. Isolation of mutations in the Drosophila homologues of the human Neurofibromatosis 2 and yeast CDC42 genes using a simple and efficient reverse-genetic method
25. Neurofibromatosis 2: Loss of merlin's protective spell
26. Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins
27. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
28. Ezrin oligomers are major cytoskeletal components of placental microvilli: A proposal for their involvement in cortical morphogenesis
29. Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains
30. Interdomain interactions of radixin in vitro
31. 2-terminal doman inhibits the cell extension activity of the COOH-terminal domain
32. Molecular dissection of radixin: Distinct and interdependent functions of the amino- and carboxy-terminal domains
33. The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
34. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
35. Structural conversion between open and closed forms of radixin: Low-angle shadowing electron microscopy
36. Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane
37. Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets
38. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
39. Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
40. Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues
41. Ezrin function is required for ROCK-mediated fibroblast transformation by the net and dbl oncogenes
42. Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility
43. Protein kinase C-θ phosphorylation of moesin in the actinbinding sequence
44. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton
45. Rho-dependent and-independent activation mechanisms of ezrin/redixin/moesin proteins: An essential role for polyphosphoinositides in vivo
46. Regulation mechanism of ERM (ezrin/redixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
47. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
48. Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides
49. Identification of a phosphatidylinositol-4, 5-bisphosphate-binding domain in the N-terminal region of ezrin
50. 2-terminal domain of ezrin correlates with its altered cellular distribution
51. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
52. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
53. The 2.7 Å crystal structure of the activated FERM domain of moesin: An analysis of structural changes on activation
54. Unexpected effects of FERM domain mutations on catalytic activity of Jak3: Structural implication for Janus kinases
55. The properties of the protein tyrosine phosphatase PTPMEG
56. F-actin binding site masked by the intramolecular association of vinculin head and tail domains
57. Actin activates a cryptic dimenzation potential of the vinculin tail domain
58. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
59. Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
60. Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
61. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
62. Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes
63. Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli
64. A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding
65. Three determinants in ezrin are responsible for cell extension activity
66. Stabilizing infrastructure of cell membranes
67. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
68. Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44
69. A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility
70. Association of ezrin with intercellular adhesion molecule-1 and-2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate
71. ICAM-2 redistributed by ezrin as a target for killer cells
72. FERMing up the synapse
73. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
74. The membrane-microfilament linker ezrin is involved in the formation of the immunological synapse and in T cell activation
75. + translocation
76. + exchanger NHE3 and the cytoskeletal protein ezrin
77. Identification of EPI64, a TBC/RabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP
78. Signal complex regulation of renal transport proteins: NHERF and regulation of NHE3 by PKA
79. New functions for the NHERF family of proteins
80. The Na-H exchanger regulatory factor
81. + exchange in OK cells
82. Ezrin is a cyclic AMP-dependent protein kinase anchoring protein
83. Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
84. An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton
85. + exchanger regulatory factor family of PDZ proteins
86. + exchange
87. A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor
88. + exchanger, NHE3, requires an associated regulatory protein
89. + exchanger regulatory factor potentiates receptor activity
90. Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton
91. Activation of ERM proteins in vivo by rho involves phosphatidylinositol 4-phosphate 5-kinase and not ROCK kinases
92. Association of the myosin-binding subunit of myosin phosphatase and moesin; dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase
93. RhoA- dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
94. Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells
95. Rho- and Rac-dependant assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
96. The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho
97. Structural basis for Neurofibromatosis type 2. Crystal structure of the medin FERM domain
98. The structure of the FERM domain of marlin, the neurofibromatosis type 2 gene product
99. Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin
100. Merlin differentially associates with the microtubule and actin cytoskeleton
101. The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association
102. Normal membrane localization and actin association of the NF2 tumor suppressor protein are dependent on folding of its N-terminal domain
103. Ezrin, radixin, and moesin are components of Schwann cell microvilli
104. Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization
105. Functional analysis of the neurofibromatosis type 2 protein by means of disease-causing point mutations
106. Interaction between two isoforms of the NF2 tumor suppressor protein, merlin, and between merlin and ezrin, suggests modulation of ERM proteins by merlin
107. Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin
108. Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF
109. Interdomain binding mediates tumor growth suppression by the NF2 gene product
110. Hierarchy of medin and eznn N- and C-terminal domain interactions in homo-and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP
111. The NF2 interactor, hepatocyte growth factor-regulated tyrosine kinase substrate (HRS), associates with merlin in the 'open' conformation and suppresses cell growth and motility
112. Expression level, subcellular distribution and Rho-GDI binding affinity of merlin in comparison with ezrin/radixin/moesin proteins
113. Neurofibromatosis 2 tumour suppressor schwannomin interacts with β11-spectrin
114. P21-activated kinase links Rao/Cdc42 signaling to Merlin
115. Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorilation on merlin localization
116. Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli
117. The Nf2 tumor suppressor, merlin, functions in Rac-dependent signaling
118. The NF2 tumor suppressor gene product, medin, mediates contact inhibition of growth through interactions with CD44
119. A systematic screen for dominant second-site modifiers of Merlin/NF2 phenotypes reveals an interaction with blistered/DSRF and scribbler
120. The FERM domain: A unique module involved in the linkage of cytoplasmic proteins to the membrane
121. CLUSTALW improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
122. Janus kinases and focal adhesion kinases play in the 4.1 band: A superfamily of band 4.1 domains important for cell structure and signal transduction
123. Comparative analysis of the Band 4.1/ezrin-related protein tyrosine phosphatase Pez from two Drosophila species: Implications for structure and function
124. Structural and evolutionary relationships among protein tyrosine phosphatase domains
125. Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors
126. Schwann cell hyperplasia and tumors in transgenic mice expressing a naturally occurring mutant NF2 protein
127. Nf2 gene inactivation in arachnoidal cells is rate-limiting for meningioma development in the mouse
128. The neurofibromatosis-2 homologue, merlin, and the tumor suppressor expanded function together in Drosophila to regulate cell proliferation and differentiation
129. CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts
130. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization
131. The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixin-moesir (ERM) family of proteins: Activation dependent binding of moesin but not ezrin
132. Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
133. Polanty and developmental regulation of two PDZ proteins in the retinal pigment epithelium
134. Ezrin links syndecan-2 to the cytoskeleton
135. Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl
136. Ezrin interacts with focal adhesion kinase and induces its activation independently of cell-matrix adhesion
137. Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway
138. CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: A novel regulatory mechanism of the CD95 apoptotic pathway
139. Characterization of human palladin, a microfilament-associated protein