Ezrin mutants affecting dimerization and activation

Biochemistry

Volumn 44, Issue 10, 2005, Pages 3926-3932

  Chambers, David N ^a,b   Bretscher, Anthony ^a  

^a Department of Obstetrics Gynecology   (United States)

^b NORTHEASTERN STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BINDING ENERGY; CYTOLOGY; DIMERIZATION; MEMBRANES; MONOMERS;

CYTOSKELETON; EZRIN; MEMBRANE-ASSOCIATED PROTEINS; MUTANTS;

PROTEINS;

EZRIN; THREONINE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIMERIZATION; GENE MUTATION; HYDRODYNAMICS; IN VIVO STUDY; LIGAND BINDING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING; WILD TYPE;

3T3 CELLS; ANIMALS; ASPARTIC ACID; BLOOD PROTEINS; CYTOSKELETAL PROTEINS; DIMERIZATION; HUMANS; LLC-PK1 CELLS; MEMBRANE PROTEINS; MICE; MICROFILAMENT PROTEINS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PHOSPHOPROTEINS; PREGNANCY PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SWINE; THREONINE;

EID: 14844366014     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0480382     Document Type: Article

References (47)

1. Bretscher, A., Edwards, K., and Fehon, R. G. (2002) ERM proteins and merlin: integrators at the cell cortex, Nat. Rev. Cell Mol. Biol. 3, 586-599.
2. Gautreau, A., Louvard, D., and Arpin, M. (2002) ERM proteins and NF2 tumor suppressor: the Yin and Yang of cortical actin organization and cell growth signaling, Curr. Opin. Cell Biol. 14, 104-9.
3. Polesello, C., and Payre, F. (2004) Small is beautiful: what flies tell us about ERM protein function in development, Trends Cell Biol. 14, 294-302.
4. Takeuchi, K., Sato, N., Kasahara, H., Funayama, N., Nagafuchi, A., Yonemura, S., Tsukita, S., and Tsukita, S. (1994) Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members, J. Cell Biol. 125, 1371-84.
5. Gould, K. L., Bretscher, A., Esch, F. S., and Hunter, T. (1989) cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1, EMBO J. 8, 4133-42.
6. Lankes, W. T., and Furthmayr, H. (1991) Moesin: a member of the protein 4.1-talin-ezrin family of proteins, Proc. Natl. Acad. Sci. U.S.A. 88, 8297-301.
7. Funayama, N., Nagafuchi, A., Sato, N., Tsukita, S., and Tsukita, S. (1991) Radixin is a novel member of the band 4.1 family, J. Cell Biol. 115, 1039-48.
8. Gary, R., and Bretscher, A. (1995) 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 6, 1061-75.
9. Reczek, D., and Bretscher, A. (1998) The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule, J. Biol. Chem. 273, 18452-8.
10. Takahashi, K., Sasaki, T., Mammoto, A., Takaishi, K., Kameyama, T., Tsukita, S., Tsukita, S., and Takai, Y. (1997) Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein, J. Biol. Chem. 272, 23371-5.
11. Yonemura, S., Hirao, M., Doi, Y., Takahashi, N., Kondo, T., Tsukita, S., and Tsukita, S. (1998) 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, J. Cell Biol. 140, 885-95.
12. Heiska, L., Alfthan, K., Gronholm, M., Vilja, P., Vaheri, A., and Carpen, O. (1998) Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5- bisphosphate, J. Biol. Chem. 273, 21893-900.
13. Parlato, S., Giammarioli, A. M., Logozzi, M., Lozupone, F., Matarrese, P., Luciani, F., Falchi, M., Malorni, W., and Fais, S. (2000) CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway, EMBO J. 19, 5123-34.
14. Serrador, J. M., Nieto, M., Alonso-Lebrero, J. L., del Pozo, M. A., Calvo, J., Furthmayr, H., Schwartz-Albiez, R., Lozano, F., Gonzalez-Amaro, R., Sanchez-Mateos, P., and Sanchez-Madrid, F. (1998) CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts, Blood 91, 4632-44.
15. Serrador, J. M., Alonso-Lebrero, J. L., del Pozo, M. A., Furthmayr, H., Schwartz-Albiez, R., Calvo, J., Lozano, F., and Sanchez-Madrid, F. (1997) Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization, J. Cell Biol. 138, 1409-23.
16. Denker, S. P., Huang, D. C., Orlowski, J., Furthmayr, H., and Barber, D. L. (2000) Direct binding of the Na⋯H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation, Mol. Cell 6, 1425-36.
17. Turunen, O., Wahlstrom, T., and Vaheri, A. (1994) Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family, J. Cell Biol. 126, 1445-53.
18. Berryman, M., and Bretscher, A. (2000) Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli, Mol. Biol. Cell 11, 1509-21.
19. Pestonjamasp, K., Amieva, M. R., Strassel, C. P., Nauseef, W. M., Furthmayr, H., and Luna, E. J. (1995) Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes, Mol. Biol. Cell 6, 247-59.
20. Martin, M., Andreoli, C., Sahuquet, A., Montcourrier, P., Algrain, M., and Mangeat, P. (1995) Ezrin NH2-terminal domain inhibits the cell extension activity of the COOH-terminal domain, J. Cell Biol. 128, 1081-93.
21. Henry, M. D., Gonzalez Agosti, C., and Solomon, F. (1995) Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains, J. Cell Biol. 129, 1007-22.
22. Pearson, M., Reczek, D., Bretscher, A., and Karplus, P. (2000) Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain, Cell 101, 259-70.
23. Finnerty, C. M., Chambers, D., Ingraffea, J., Faber, H. R., Karplus, P. A., and Bretscher, A. (2004) The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain, J. Cell Sci. 117, 1547-52.
24. Smith, W. J., Nassar, N., Bretscher, A., Cerione, R. A., and Karplus, P. A. (2003) Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions, J. Biol. Chem. 278, 4949-56.
25. Hamada, K., Matsui, T., Tsukita, S., and Hakoshima, T. (2000) Crystallographic characterization of the membrane-binding domain of radixin, Acta Crystallogr., Sect. D 56, 922-3.
26. Edwards, S. D., and Keep, N. H. (2001) The 2.7 Å crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation, Biochemistry 40, 7061-8.
27. Nakamura, F., Amieva, M. R., and Furthmayr, H. (1995) Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets, J. Biol. Chem. 270, 31377-85.
28. Matsui, T., Maeda, M., Doi, Y., Yonemura, S., Amano, M., Kaibuchi, K., Tsukita, S., and Tsukita, S. (1998) Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association, J. Cell Biol. 140, 647-57.
29. Nakamura, F., Huang, L., Pestonjamasp, K., Luna, E. J., and Furthmayr, H. (1999) Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides, Mol. Biol. Cell 10, 2669-85.
30. Simons, P. C., Pietromonaco, S. F., Reczek, D., Bretscher, A., and Elias, L. (1998) C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton, Biochem. Biophys. Res. Commun. 253, 561-5.
31. Fievet, B. T., Gautreau, A., Roy, C., Del Maestro, L., Mangeat, P., Louvard, D., and Arpin, M. (2004) Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism ofezrin, J. Cell Biol. 164, 653-9.
32. Oshiro, N., Fukata, Y., and Kaibuchi, K. (1998) Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures, J. Biol. Chem. 273, 34663-6.
33. Gautreau, A., Louvard, D., and Arpin, M. (2000) Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane, J. Cell Biol. 150, 193-203.
34. Gary, R., and Bretscher, A. (1993) Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins, Proc. Natl. Acad. Sci. U.S.A. 90, 10846-50.
35. Berryman, M., Gary, R., and Bretscher, A. (1995) Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis, J. Cell Biol. 131, 1231-42.
36. Bretscher, A., Gary, R., and Berryman, M. (1995) Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains, Biochemistry 34, 16830-7.
37. Turunen, O., Sainio, M., Jaaskelainen, J., Carpen, O., and Vaheri, A. (1998) Structure-function relationships in the ezrin family and the effect of tumor-associated point mutations in neurofibromatosis 2 protein, Biochim. Biophys. Acta 1387, 1-16.
38. Reczek, D., Berryman, M., and Bretscher, A. (1997) Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family, J. Cell Biol. 139, 169-79.
39. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-5.
40. Bretscher, A. (1983) Microfilament organization in the cytoskeleton of the intestinal brush border, Cell Muscle Motil. 4, 239-68.
41. Siegel, L. M., and Monty, K. J. (1966) Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases, Biochim. Biophys. Acta 112, 346-62.
42. Bretscher, A. (1983) Purification of an 80 000 Da protein that is a component of the isolated microvillus cytoskeleton and its localization in nonmuscle cells, J. Cell Biol. 97, 425-32.
43. Ishikawa, H., Tamura, A., Matsui, T., Sasaki, H., Hakoshima, T., and Tsukita, S. (2001) Structural conversion between open and closed forms of radixin: low-angle shadowing electron microscopy, J. Mol. Biol. 310, 973-8.
44. Hoeflich, K. P., Tsukita, S., Hicks, L., Kay, C. M., and Ikura, M. (2003) Insights into a single rodlike helix in activated radixin required for membrane-cytoskeletal cross-linking, Biochemistry 42, 11634-41.
45. Melby, T. E., Ciampaglio, C. N., Briscoe, G., and Erickson, H. P. (1998) The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge, J. Cell Biol. 142, 1595-604.
46. Dransfield, D. T., Bradford, A. J., Smith, J., Martin, M., Roy, C., Mangeat, P. H., and Goldenring, J. R. (1997) Ezrin is a cyclic AMP-dependent protein kinase anchoring protein, EMBO J. 16, 35-43.
47. Nguyen, R., Reczek, D., and Bretscher, A. (2001) Hierarchy of merlin and ezrin N- and C-terminal domain interactions in homo-and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP, J. Biol. Chem. 276, 7621-9.