ERM (ezrin/radixin/moesin) family: From cytoskeleton to signal transduction

Current Opinion in Cell Biology

Volumn 9, Issue 1, 1997, Pages 70-75

  Tsukita, Sachiko ^a   Yonemura, Shigenobu ^a   Tsukita, Shoichiro ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; EZRIN; MOESIN; RADIXIN;

CYTOSKELETON; HUMAN; MOUSE; NEUROFIBROMATOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; SEQUENCE HOMOLOGY; SHORT SURVEY; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; TUMOR SUPPRESSOR GENE;

EID: 0031043523     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80154-8     Document Type: Article

References (42)

1. 1. Arpin M, Algrain M, Louvard D: Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1. Curr Opin Cell Biol 1994, 6:136-141.
2. 2. Takeuchi K, Kawashima A, Nagafuchi A, Tsukita Sh: Structural diversity of band 4.1 superfamily members. J Cell Sci 1994, 107:1921-1928.
3. 3. Winckler B, Gonzalez Agosti C, Magendantz M, Solomon F: Analysis of a cortical cytoskeletal structure: a role for ezrin-radixin-moesin (ERM proteins) in the marginal band of chicken erythrocytes. J Cell Sci 1994, 107:2523-2534.
4. 4. Dunster LM, Schneider-Schaulies J, Loffler S, Lankes W, Schwartz-Albiez R, Lottspeich F, Meulen V: Moesin: a cell membrane protein linked with susceptibility to measles virus infection. Virology 1994, 198:265-274.
5. 5. Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, Krohne G, Meulen V: Physical association of moesin and CD46 as a receptor complex for measles virus. J Virol 1995, 69:2248-2256.
6. 6. Sagara J, Tsukita Sa, Yonemura S, Tsukita Sh, Kawai A: Cellular actin-binding ezrin-radixin-moesin (ERM) family proteins are incorporated into the rabies virion and closely associated with viral envelope proteins in the cell. Virology 1995, 206:485-494.
7. 7. Helander TS, Carpén O, Turunen O, Kovanen PE, Vaheri A, Timonen T: ICAM-2 redistributed by ezrin as a target for killer cells. Nature 1996, 382:265-268.
8. 8. Takeuchi K, Sato N, Kasahara H, Funayama N, Nagafuchi A, Yonemura S, Tsukita Sa, Tsukita Sh: Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J Cell Biol 1994, 125:1371-1384.
9. 9. Martin M, Andreoli C, Sahuquet A, Montcourrier P, Algrain M, Mangeat P: Ezrin NH2-terminal domain inhibits the cell extension activity of the COOH-terminal domain. J Cell Biol 1995, 128:1081-1093.
10. 10. Henry MD, Gonzalez Agosti C, Solomon F: Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains. J Cell Biol 1995, 129:1007-1022. The authors of this paper suggest the distinct functions of the amino- and carboxy-terminal domains of radixin by means of transfection experiments. It is suggested that the functions of radixin in cells depend upon activities contributed by these two domains of the protein through modulating interactions between those domains.
11. 11. Edwards KA, Montague RA, Shepard S, Edgar BA, Erikson RL, Kiehart DP: Identification of Drosophila cytoskeletal proteins by induction of abnormal cell shape in fission yeast. Proc Natl Acad Sci USA 1994, 91:4589-4593.
12. 12. Turunen O, Wahlstrom T, Vaheri A: Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J Cell Biol 1994, 126:1445-1453.
13. 13. Pestonjamasp K, Amieva MR, Strassel CP, Nauseef WM, Furthmayr H, Luna EJ: Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes. Mol Biol Cell 1995, 6:247-259.
14. 14. Tsukita Sa, Oishi K, Sato N, Sagara J, Kawai A, Tsukita Sh: ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 1994, 126:391-401.
15. 15. Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita Sh, Tsukita Sa: Regulation mechanism of ERM protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and rho-dependent signaling pathway. J Cell Biol 1996, 135:37-52. CD44 was identified as amembrane-binding partner of ERM proteins in BHK and L cells by immunoprecipitation using anti-moesin monoclonal antibody [14]. This paper [15**] shows that the binding of ERM proteins to the cytoplasmic domain of CD44 is regulated by phosphoinositides in vitro, and also provides evidence that Rho regulates the formation of the CD44-ERM complex.
16. 16. Berryman M, Gary R, Bretscher A: Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis. J Cell Biol 1995, 131:1231-1242. Shows that ezrin is a major component of isolated placental microvilli, where it exists primarily in oligomeric form, being cytoskeletally associated. This paper also describes the rapid formation of ezrin oligomers after tyrosine phosphorylation of ezrin in EGF-stimulated A431 cells.
17. 17. Driessens MHE, Stroeken PJM, Rodriguez Erena NF, Van der Valk MA, Van Rijthoven EAM, Roos E: Targeted disruption of CD44 in MDAY-D2 lymphosarcoma cells has no effect on subcutaneous growth or metastatic capacity. J Cell Biol 1995, 131:1849-1855.
18. 18. Yao X, Cheng L, Forte JG: Biochemical characterization of ezrin-actin interaction. J Biol Chem 1996, 271:7224-7229.
19. 19. Shuster CB, Herman IM: Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity. J Cell Biol 1995, 128:837-848.
20. 20. Bretscher A, Gary R, Berryman M: Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains. Biochemistry 1995, 34:16830-16837.
21. 21. Gary R, Bretscher A: Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins. Proc Natl Acad Sci USA 1993, 90:10846-10850.
22. 22. Gary R, Bretscher A: Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol Biol Cell 1995, 6:1061-1075.
23. 23. Andreoli C, Martin M, Le Borgne R, Reggio H, Mangeat P: Ezrin has properties to self-associate at the plasma membrane. J Cell Sci 1994, 107:2509-2521.
24. 24. Magendantz M, Henry MD, Lander A, Solomon F: Interdomain interactions of radixin in vitro. J Biol Chem 1995, 270:25324-25327.
25. 25. Takeda H, Nagafuchi A, Yonemura S, Tsukita Sa, Behrens J, Birchmeier W, Tsukita Sh: V-src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and beta catenin is not required for the shift. J Cell Biol 1995, 131:1839-1847.
26. 26. Jiang WG, Hiscox S, Singhrao SK, Puntis MC, Nakamura T, Mansel RE, Hallettt MB: Induction of tyrosine phosphorylation and translocation of ezrin by hepatocyte growth factor/scatter factor. Biochem Biophys Res Commun 1995, 217:1062-1069.
27. 27. Nakamura F, Amieva MR, Furthmayr H: Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. J Biol Chem 1995, 270:31377-31385. Reports the phosphorylation and localization of moesin during early steps of platelet activation by thrombin. Upon exposure to thrombin, phosphorylation of Thr558 of moesin remarkably increases, with drastic cytoskeletal rearrangement resulting, thus suggesting a model for regulated membrane-cytoskeleton interactions through moesin during platelet activation.
28. 28. Chen J, Cohn JA, Mandel LJ: Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury. Proc Natl Acad Sci USA 1995, 92:7495-7499.
29. 29. Niggli V, Andreoli C, Roy C, Mangeat P: Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett 1995, 376:172-176.
30. 30. Takaishi K, Sasaki T, Kameyama T, Tsukita Sa, Tsukita Sh, Takai Y: Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene 1995, 11:39-48.
31. 31. Nagata K, Hall A: The Rho GTPase regulates protein kinase activity. Bioessays 1996, 18:529-531.
32. 32. Thomas G, Merel P, Sanson K, Hoang-Xuan K, Zucman J, Desmaze C, Melot T, Aurias A, Delattre O: Neurofibromatosis type 2. Eur J Cancer 1994, 13:1981-1987.
33. 33. Den Bakker MA, Riegman PH, Hekman RA, Boersma W, Janssen PJ, Van der Kwast TH, Zwarthoff EC: The product of the NF2 tumour suppressor gene localizes near the plasma membrane and is highly expressed in muscle cells. Oncogens 1995, 10:757-763.
34. 34. Sainz J, Huynh DP, Figueroa K, Ragge NK, Baser ME, Pulst SM: Mutations of the neurofibromatosis type 2 gene and lack of the gene product in vestibular schwannomas. Hum Mol Genet 1994, 3:885-891.
35. 35. Gonzalez-Agosti C, Xu L, Pinney D, Beauchamp R, Hobbs W, Gusella J, Ramesh V: The merlin tumor suppressor localizes preferentially in membrane ruffles. Oncogene 1997, 13:in press.
36. 36. Takeshima H, Izawa I, Lee PS, Safdar N, Levin VA, Saya H: Detection of cellular proteins that interact with the NF2 tumor suppressor gene product. Oncogene 1994, 9:2135-2144.
37. 37. Lutchman M, Rouleau G: The neurofibromatosis type 2 gene product, schwannomin, suppresses growth of NIH3T3 cells. Cancer Res 1995, 55:2270-2274.
38. 38. Huynh DP, Pulst SM: Neurofibromatosis 2 antisense oligonucleotides induce reversible inhibition of schwannomin synthesis and cell adhesion in STS26T and T98G cells. Oncogene 1996, 13:73-84.
39. 39. McCartney BM, Fehon RG: Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin. J Cell Biol 1996, 133:843-852. Identifies and characterizes Drosophila homologues of moesin and of merlin, which show distinct subcellular localizations. It has been suggested that merlin has unique functions in the cell which differ from those of other ERM proteins.
40. 40. Tikoo A, Varga M, Ramesh V, Gusella J, Maruta H: An anti-Ras function of neurofibromatosis type 2 gene product (NF2/Merlin). J Biol Chem 1994, 269:23387-23390.
41. 41. Amieva MR, Wilgenbus KK, Furthmayr H: Radixin is a component of hepatocyte microvili in situ. Exp Cell Res 1994, 210:140-144.
42. 42. Schwartz AR, Merling A, Spring H, Moller P, Koretz K: Differential expression of the microspike-associated protein moesin in human tissues. Eur J Cell Biol 1995, 67:189-198.