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Volumn 10, Issue 8, 1999, Pages 2669-2685

Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides

Author keywords

[No Author keywords available]

Indexed keywords

CALYCULIN A; DETERGENT; F ACTIN; MOESIN; POLYPHOSPHOINOSITIDE; STAUROSPORINE; THREONINE; THROMBIN;

EID: 0032783917     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.8.2669     Document Type: Article
Times cited : (128)

References (95)
  • 1
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain, M., Turunen, O., Vaheri, A., Louvard, D., and Arpin, M. (1993). Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120, 129-139.
    • (1993) J. Cell Biol. , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 2
    • 0029086637 scopus 로고
    • Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts
    • Amieva, M.R., and Furthmayr, H. (1995). Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. Exp. Cell Res. 219, 180-196.
    • (1995) Exp. Cell Res. , vol.219 , pp. 180-196
    • Amieva, M.R.1    Furthmayr, H.2
  • 3
    • 0032949862 scopus 로고    scopus 로고
    • Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrin: In vivo imaging with GFP fusion proteins
    • Amieva, M.R., Litman, P., Huang, L., Ichimaru, E., and Furthmayr, H. (1998). Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrin: in vivo imaging with GFP fusion proteins. J. Cell Sci. 122, 111-125.
    • (1998) J. Cell Sci. , vol.122 , pp. 111-125
    • Amieva, M.R.1    Litman, P.2    Huang, L.3    Ichimaru, E.4    Furthmayr, H.5
  • 4
    • 0028923464 scopus 로고
    • The thrombin receptor in human platelets is coupled to a GTP binding protein of the G alpha q family
    • Benka, M.L., et al. (1995). The thrombin receptor in human platelets is coupled to a GTP binding protein of the G alpha q family. FEBS Lett. 363, 49-52.
    • (1995) FEBS Lett. , vol.363 , pp. 49-52
    • Benka, M.L.1
  • 5
    • 0024542907 scopus 로고
    • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A431 cells by epidermal growth factor
    • Bretscher, A. (1989). Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A431 cells by epidermal growth factor. J. Cell Biol. 108, 921-930.
    • (1989) J. Cell Biol. , vol.108 , pp. 921-930
    • Bretscher, A.1
  • 6
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher, A. (1999). Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr. Opin. Cell Biol. 11, 109-116.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 7
    • 0029609581 scopus 로고
    • Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains
    • 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, 16830-16837.
    • (1995) Biochemistry , vol.34 , pp. 16830-16837
    • Bretscher, A.1    Gary, R.2    Berryman, M.3
  • 8
    • 0030820404 scopus 로고    scopus 로고
    • Signal transduction pathways involving the small G proteins rac and Cdc42 and phosphoinositide kinases
    • Carpenter, C.L., Tolias, K.F., Couvillon, A.C., and Hartwig, J.H. (1997). Signal transduction pathways involving the small G proteins rac and Cdc42 and phosphoinositide kinases. Adv. Enzyme Regul. 37, 377-390.
    • (1997) Adv. Enzyme Regul. , vol.37 , pp. 377-390
    • Carpenter, C.L.1    Tolias, K.F.2    Couvillon, A.C.3    Hartwig, J.H.4
  • 9
    • 0020082617 scopus 로고
    • Phosphorylation of platelet actin-binding protein during platelet activation
    • Carroll, R.C., and Gerrard, J.M. (1982). Phosphorylation of platelet actin-binding protein during platelet activation. Blood 59, 466-471.
    • (1982) Blood , vol.59 , pp. 466-471
    • Carroll, R.C.1    Gerrard, J.M.2
  • 10
    • 0029084127 scopus 로고
    • Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury
    • Chen, J., Cohn, J.A., and Mandel, L.J. (1995). Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury. Proc. Natl. Acad. Sci. USA 92, 7495-7499.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7495-7499
    • Chen, J.1    Cohn, J.A.2    Mandel, L.J.3
  • 11
    • 0026026620 scopus 로고
    • Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein
    • Chia, C.P., Hitt, A.L., and Luna, E.J. (1991). Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein. Cell Motil. Cytoskeleton 18, 164-179.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 164-179
    • Chia, C.P.1    Hitt, A.L.2    Luna, E.J.3
  • 12
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L.D., Traynor-Kaplan, A., Bokoch, G.M., and Schwartz, M.A. (1994). The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79, 507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 13
    • 0027340192 scopus 로고
    • Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets
    • Clark, E.A., and Brugge, J.S. (1993). Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol. Cell. Biol. 13, 1863-1871.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1863-1871
    • Clark, E.A.1    Brugge, J.S.2
  • 14
    • 0030763919 scopus 로고    scopus 로고
    • Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
    • Crepaldi, T., Gautreau, A., Comoglio, P.M., Louvard, D., and Arpin, M. (1997). Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells. J. Cell Biol. 138, 423-434.
    • (1997) J. Cell Biol. , vol.138 , pp. 423-434
    • Crepaldi, T.1    Gautreau, A.2    Comoglio, P.M.3    Louvard, D.4    Arpin, M.5
  • 15
    • 0027255099 scopus 로고
    • Rapid phosphorylation and selective dephosphorylation of P-selectin accompanies platelet activation
    • Crovello, C.S., Furie, B.C., and Furie, B. (1993). Rapid phosphorylation and selective dephosphorylation of P-selectin accompanies platelet activation. J. Biol. Chem. 268, 14590-14593.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14590-14593
    • Crovello, C.S.1    Furie, B.C.2    Furie, B.3
  • 16
    • 0026697728 scopus 로고
    • Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells
    • Egerton, M., Burgess, W.H., Chen, D., Druker, B.J., Bretscher, A., and Samelson, L.E. (1992). Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells. J. Immunol. 149, 1847-1852.
    • (1992) J. Immunol. , vol.149 , pp. 1847-1852
    • Egerton, M.1    Burgess, W.H.2    Chen, D.3    Druker, B.J.4    Bretscher, A.5    Samelson, L.E.6
  • 17
    • 0024996471 scopus 로고
    • Staurosporine inhibits a tyrosine protein kinase in human hepatoma cell membranes
    • Fallon, R.J. (1990). Staurosporine inhibits a tyrosine protein kinase in human hepatoma cell membranes. Biochem. Biophys. Res. Commun. 170, 1191-1196.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1191-1196
    • Fallon, R.J.1
  • 18
    • 0027196725 scopus 로고
    • The ezrin-like family of tyrosine kinase substrates: Receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation
    • Fazioli, F., Wong, W.T., Ullrich, S.J., Sakaguchi, K., Appella, E., and Di Fiore, P.P. (1993). The ezrin-like family of tyrosine kinase substrates: receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation. Oncogene 8, 1335-1345.
    • (1993) Oncogene , vol.8 , pp. 1335-1345
    • Fazioli, F.1    Wong, W.T.2    Ullrich, S.J.3    Sakaguchi, K.4    Appella, E.5    Di Fiore, P.P.6
  • 19
    • 0023766362 scopus 로고
    • Platelet tyrosine-specific protein phosphorylation is regulated by thrombin
    • Ferrell, J.E., Jr., and Martin, G.S. (1988). Platelet tyrosine-specific protein phosphorylation is regulated by thrombin. Mol. Cell. Biol. 8, 3603-3610.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3603-3610
    • Ferrell J.E., Jr.1    Martin, G.S.2
  • 20
    • 0027748236 scopus 로고
    • The platelet cytoskeleton
    • Fox, J.E. (1993). The platelet cytoskeleton. Thromb. Haemost. 70, 884-893.
    • (1993) Thromb. Haemost. , vol.70 , pp. 884-893
    • Fox, J.E.1
  • 21
    • 0027444694 scopus 로고
    • On the role of the platelet membrane skeleton in mediating signal transduction. Association of GP Ilb-IIIa, pp60c-src, pp62c-yes, and the p21ras GTPase-activating protein with the membrane skeleton
    • Fox, J.E., Lipfert, L., Clark, E.A., Reynolds, C.C., Austin, C.D., and Brugge, J.S. (1993). On the role of the platelet membrane skeleton in mediating signal transduction. Association of GP Ilb-IIIa, pp60c-src, pp62c-yes, and the p21ras GTPase-activating protein with the membrane skeleton. J. Biol. Chem. 268, 25973-25984.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25973-25984
    • Fox, J.E.1    Lipfert, L.2    Clark, E.A.3    Reynolds, C.C.4    Austin, C.D.5    Brugge, J.S.6
  • 22
    • 0019941979 scopus 로고
    • Role of phosphorylation in mediating the association of myosin with the cytoskeletal structures of human platelets
    • Fox, J.E., and Phillips, D.R. (1982). Role of phosphorylation in mediating the association of myosin with the cytoskeletal structures of human platelets. J. Biol. Chem. 257, 4120-4126.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4120-4126
    • Fox, J.E.1    Phillips, D.R.2
  • 23
    • 0026756594 scopus 로고
    • Requirements of phosphatidylinositol 4,5-biphosphate for alpha-actinin function [see comments]
    • Fukami, K., Furuhashi, K., Ingaki, M., Endo, T., Hatano, S., and Takenawa, T. (1992). Requirements of phosphatidylinositol 4,5-biphosphate for alpha-actinin function [see comments]. Nature 359, 150-152.
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Ingaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 25
    • 0026683647 scopus 로고
    • Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin
    • Furuhashi, K., Inagaki, M., Hatano, S., Fukami, K., and Takenawa, T. (1992). Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin. Biochem. Biophys. Res. Commun. 184, 1261-1265.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1261-1265
    • Furuhashi, K.1    Inagaki, M.2    Hatano, S.3    Fukami, K.4    Takenawa, T.5
  • 26
    • 0029121577 scopus 로고
    • 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., 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, 1061-1075.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 27
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-biphosphate
    • Gilmore, A.P., and Burridge, K. (1996). Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-biphosphate. Nature 38, 531-535.
    • (1996) Nature , vol.38 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 28
    • 0017712880 scopus 로고
    • Comparative biochemistry of non-muscle actins
    • Gordon, D.J., Boyer, J.L., and Korn, E.D. (1977). Comparative biochemistry of non-muscle actins. J. Biol. Chem. 252, 8300-8309.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8300-8309
    • Gordon, D.J.1    Boyer, J.L.2    Korn, E.D.3
  • 29
    • 0024814175 scopus 로고
    • cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1
    • 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, 4133-4142.
    • (1989) EMBO J. , vol.8 , pp. 4133-4142
    • Gould, K.L.1    Bretscher, A.2    Esch, F.S.3    Hunter, T.4
  • 30
    • 0022589111 scopus 로고
    • The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein
    • Gould, K.L., Cooper, J.A., Bretscher, A., and Hunter, T. (1986). The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein. J. Cell Biol. 102, 660-669.
    • (1986) J. Cell Biol. , vol.102 , pp. 660-669
    • Gould, K.L.1    Cooper, J.A.2    Bretscher, A.3    Hunter, T.4
  • 31
    • 0025769919 scopus 로고
    • The secretion-stimulated 80 k phosphoprotein of parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the indiced apical microvilli
    • Hanzel, D., Reggio, H., Bretscher, A., Forte, J.G., and Mangeat, P. (1991). The secretion-stimulated 80 k phosphoprotein of parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the indiced apical microvilli. EMBO J. 10, 2363-2373.
    • (1991) EMBO J. , vol.10 , pp. 2363-2373
    • Hanzel, D.1    Reggio, H.2    Bretscher, A.3    Forte, J.G.4    Mangeat, P.5
  • 32
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated rac uncap actin filament barbed ends through PI synthesis in permeabilized human platelets
    • Hartwig, J.H., Bokoch, J.M., Carpenter, C.L., Janmey, P.A., Taylor, L.A., Toker, A., and Stossel, T.P. (1995). Thrombin receptor ligation and activated rac uncap actin filament barbed ends through PI synthesis in permeabilized human platelets. Cell 82, 643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, J.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 34
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao, M., Sato, N., Kondo, T., Yonemura, S., Monden, M., Sasaki, T., Takai, Y., Tsukita, S., and Tsukita, S. (1996). Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 235, 37-51.
    • (1996) J. Cell Biol. , vol.235 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 35
    • 0024519908 scopus 로고
    • Measurement of secretion of adenine nucleotides
    • Holmsen, H., and Dangelmaier, C.A. (1989). Measurement of secretion of adenine nucleotides. Methods Enzymol. 169, 195-205.
    • (1989) Methods Enzymol. , vol.169 , pp. 195-205
    • Holmsen, H.1    Dangelmaier, C.A.2
  • 37
    • 0033617289 scopus 로고    scopus 로고
    • 558threonine, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin: Regulation of conformational change
    • 558threonine, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin: regulation of conformational change. J. Biol. Chem. 274, 12803-12810.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12803-12810
    • Huang, L.1    Wong, T.Y.W.2    Lin, R.W.W.3    Furthmayr, H.4
  • 38
    • 85038156337 scopus 로고
    • ed. T. Yoshida, S. Shindo, T. Ohgaki and T. Yamanaka, Tokyo: Kogakutosho
    • Igarashi, T. (1987). In: Handbook of Surfactants, ed. T. Yoshida, S. Shindo, T. Ohgaki and T. Yamanaka, Tokyo: Kogakutosho, 116-139.
    • (1987) Handbook of Surfactants , pp. 116-139
    • Igarashi, T.1
  • 39
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P.A. (1994). Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56, 169-191.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 40
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R.P., and Craig, S.W. (1994). F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373, 261-264.
    • (1994) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 41
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson, R.P., and Craig, S.W. (1995). An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269, 12611-12619.
    • (1995) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 42
    • 0030222341 scopus 로고    scopus 로고
    • Crosstalk between cell adhesion molecules: Vinculin as a paradigm for regulation by conformation
    • Joust, B., and Rudiger, M. (1998). Crosstalk between cell adhesion molecules: vinculin as a paradigm for regulation by conformation. Trends Cell Biol. 6, 311-315.
    • (1998) Trends Cell Biol. , vol.6 , pp. 311-315
    • Joust, B.1    Rudiger, M.2
  • 43
    • 0020962197 scopus 로고
    • Synergistic functions of protein phosphorylation and calcium mobilization in platelet activation
    • Kaibuchi, K., Takai, Y., Sawamura, M., Hoshijima, M., Fujikura, T., and Nishizuka, Y. (1983). Synergistic functions of protein phosphorylation and calcium mobilization in platelet activation. J. Biol. Chem. 258, 6701-6704.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6701-6704
    • Kaibuchi, K.1    Takai, Y.2    Sawamura, M.3    Hoshijima, M.4    Fujikura, T.5    Nishizuka, Y.6
  • 44
    • 0023153357 scopus 로고
    • Head group and chain length dependence of phospholipid self-assembly studied by spin-label electron spin resonance
    • King, M.D., and Marsh, D. (1987). Head group and chain length dependence of phospholipid self-assembly studied by spin-label electron spin resonance. Biochemistry 26, 1224-1231.
    • (1987) Biochemistry , vol.26 , pp. 1224-1231
    • King, M.D.1    Marsh, D.2
  • 45
    • 0030961752 scopus 로고    scopus 로고
    • Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells
    • Kotani, H., Takaishi, K., Sasaki, T., and Takai, Y. (1997). Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells. Oncogene 14, 1705-1713.
    • (1997) Oncogene , vol.14 , pp. 1705-1713
    • Kotani, H.1    Takaishi, K.2    Sasaki, T.3    Takai, Y.4
  • 46
    • 0026760578 scopus 로고
    • Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin
    • Krieg, J., and Hunter, T. (1992). Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin. J. Biol. Chem. 267, 19258-19265.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19258-19265
    • Krieg, J.1    Hunter, T.2
  • 47
    • 0020475449 scopus 로고
    • A method for displaying the hydrophathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982). A method for displaying the hydrophathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 48
    • 0031240066 scopus 로고    scopus 로고
    • Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts
    • Lamb, R.F., Ozanne, B.W., Roy, C., McGarry, L., Stipp, C., Mangeat, P., and Jay, D.G. (1997). Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts. Curr. Biol. 7, 682-688.
    • (1997) Curr. Biol. , vol.7 , pp. 682-688
    • Lamb, R.F.1    Ozanne, B.W.2    Roy, C.3    McGarry, L.4    Stipp, C.5    Mangeat, P.6    Jay, D.G.7
  • 49
    • 0344643940 scopus 로고
    • A heparin-binding protein involved in inhibition of smooth muscle cell proliferation
    • Lankes, W., Griesmacher, A., Gruenwald, J., Schwartz-Albiez, R., and Keller, R. (1988). A heparin-binding protein involved in inhibition of smooth muscle cell proliferation. Eur. J. Biochem. 252, 831-842.
    • (1988) Eur. J. Biochem. , vol.252 , pp. 831-842
    • Lankes, W.1    Griesmacher, A.2    Gruenwald, J.3    Schwartz-Albiez, R.4    Keller, R.5
  • 50
    • 0027745661 scopus 로고
    • Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains
    • Lankes, W., Schwartz-Albiez, R., and Furthmayr, H. (1993). Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains. Biochim. Biophys. Acta 1216, 479-482.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 479-482
    • Lankes, W.1    Schwartz-Albiez, R.2    Furthmayr, H.3
  • 51
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-talin-ezrin family of proteins
    • Lankes, W.T., and Furthmayr, H. (1991). Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Proc. Natl. Acad. Sci. USA 88, 8297-8301.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8297-8301
    • Lankes, W.T.1    Furthmayr, H.2
  • 52
    • 0032482323 scopus 로고    scopus 로고
    • Identification and functional analysis of the ezrin-binding site in the hyaluran receptor, CD44
    • Legg, J.W., and Isacke, C.M. (1998). Identification and functional analysis of the ezrin-binding site in the hyaluran receptor, CD44. Curr. Biol. 8, 705-708.
    • (1998) Curr. Biol. , vol.8 , pp. 705-708
    • Legg, J.W.1    Isacke, C.M.2
  • 53
    • 0026497659 scopus 로고
    • Integral-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
    • Lipfert, L., Haimovich, B., Schaller, M.D., Cobb, B.S., Parsons, J.T., and Brugge, J.S. (1992). Integral-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J. Cell Biol. 119, 905-912.
    • (1992) J. Cell Biol. , vol.119 , pp. 905-912
    • Lipfert, L.1    Haimovich, B.2    Schaller, M.D.3    Cobb, B.S.4    Parsons, J.T.5    Brugge, J.S.6
  • 54
    • 0031032599 scopus 로고    scopus 로고
    • Selective recognition of phosphatidylinositol 3,4,5-triphosphate by a synthetic peptide
    • Lu, P.J., and Chen, C.S. (1997). Selective recognition of phosphatidylinositol 3,4,5-triphosphate by a synthetic peptide. J. Biol. Chem. 272, 466-472.
    • (1997) J. Biol. Chem. , vol.272 , pp. 466-472
    • Lu, P.J.1    Chen, C.S.2
  • 55
    • 0030872949 scopus 로고    scopus 로고
    • Rho and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ERM proteins
    • Mackay, D.J.G., Esch, F., Furthmayr, H., and Hall, A. (1997). Rho and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ERM proteins. J. Cell Biol. 138, 927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.G.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 56
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in rac- and rho-induced cytoskeletal reorganization
    • Machesky, L.M., and Hall, A. (1997). Role of actin polymerization and adhesion to extracellular matrix in rac- and rho-induced cytoskeletal reorganization. J. Cell Biol. 138, 913-926.
    • (1997) J. Cell Biol. , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 59
    • 0032498528 scopus 로고    scopus 로고
    • 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., 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, 647-657.
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7    Tsukita, S.8
  • 60
    • 0024379951 scopus 로고
    • A derivative of staurosporine (CGP 41 251) shows selectivity for protein kinase C inhibition and in vitro anti-proliferative as well as in vivo anti-rumor activity
    • Meyer, T., Regenass, U., Fabbro, D., Alteri, E., Rosel, J., Muller, M., Caravatti, G., and Matter, A. (1989). A derivative of staurosporine (CGP 41 251) shows selectivity for protein kinase C inhibition and in vitro anti-proliferative as well as in vivo anti-rumor activity. Int. J. Cancer 43, 851-856.
    • (1989) Int. J. Cancer , vol.43 , pp. 851-856
    • Meyer, T.1    Regenass, U.2    Fabbro, D.3    Alteri, E.4    Rosel, J.5    Muller, M.6    Caravatti, G.7    Matter, A.8
  • 61
    • 0024109183 scopus 로고
    • Cytoskeletal dynamics and nerve growth
    • Mitchison, T., and Kirschner, M. (1988). Cytoskeletal dynamics and Nerve Growth. Neuron 1, 761-822.
    • (1988) Neuron , vol.1 , pp. 761-822
    • Mitchison, T.1    Kirschner, M.2
  • 62
    • 0027963391 scopus 로고
    • Role of type 1 and type 2A phosphatases in signal transduction of platelet-activating-factor-stimulated rabbit platelets
    • Murphy, C.T., and Westwick, J. (1994). Role of type 1 and type 2A phosphatases in signal transduction of platelet-activating-factor-stimulated rabbit platelets. Biochem. J. 301, 531-537.
    • (1994) Biochem. J. , vol.301 , pp. 531-537
    • Murphy, C.T.1    Westwick, J.2
  • 63
    • 0029569120 scopus 로고
    • Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets
    • 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, 31377-31385.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31377-31385
    • Nakamura, F.1    Amieva, M.R.2    Furthmayr, H.3
  • 64
    • 0030600351 scopus 로고    scopus 로고
    • Phosphorylarion of 558T of moesin detected by site-specific antibodies in RAW264.7 macrophages
    • Nakamura, F., Amieva, M.R., Hirota, C., Mizuno, Y., and Furthmayr, H. (1996). Phosphorylarion of 558T of moesin detected by site-specific antibodies in RAW264.7 macrophages. Biochem. Biophys. Res. Commun. 226, 650-656.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 650-656
    • Nakamura, F.1    Amieva, M.R.2    Hirota, C.3    Mizuno, Y.4    Furthmayr, H.5
  • 65
    • 0023258497 scopus 로고
    • Staurosporine inhibits tyrosine-specific protein kinase activity of Rous sarcoma virus transforming protein p60
    • Nakano, H., Kobayashi, E., Takahashi, I., Tamaoki, T., Kuzuu, Y., and Iba, H. (1987). Staurosporine inhibits tyrosine-specific protein kinase activity of Rous sarcoma virus transforming protein p60. J. Antibiot. 40, 706-708.
    • (1987) J. Antibiot. , vol.40 , pp. 706-708
    • Nakano, H.1    Kobayashi, E.2    Takahashi, I.3    Tamaoki, T.4    Kuzuu, Y.5    Iba, H.6
  • 66
    • 0028800154 scopus 로고
    • Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin
    • Niggli, V., Andreoli, C., Roy, C., and Mangeat, P. (1995). Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett. 376, 172-176.
    • (1995) FEBS Lett. , vol.376 , pp. 172-176
    • Niggli, V.1    Andreoli, C.2    Roy, C.3    Mangeat, P.4
  • 67
    • 0028302211 scopus 로고
    • Role of platelets in thrombosis and hemostasis
    • Packham, M.A. (1994). Role of platelets in thrombosis and hemostasis. Can. J. Physiol. Pharmacol. 72, 278-284.
    • (1994) Can. J. Physiol. Pharmacol. , vol.72 , pp. 278-284
    • Packham, M.A.1
  • 68
    • 0032547839 scopus 로고    scopus 로고
    • Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons
    • Paglini, G., Kunda, P., Quiroga, S., Kosik, K., and Caceras, A. (1998). Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons. J. Cell Biol. 143, 443-455.
    • (1998) J. Cell Biol. , vol.143 , pp. 443-455
    • Paglini, G.1    Kunda, P.2    Quiroga, S.3    Kosik, K.4    Caceras, A.5
  • 69
    • 0038938785 scopus 로고    scopus 로고
    • Crystallographic studies of moesin: A protein that links the actin cytoskeleton to the plasma membrane
    • Abstract
    • Pearson, M., Reczek, D., Bretscher, A., and Karplus, P.A. (1998). Crystallographic studies of moesin: a protein that links the actin cytoskeleton to the plasma membrane. Mol. Biol. Cell 9, 265a (Abstract).
    • (1998) Mol. Biol. Cell , vol.9
    • Pearson, M.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 70
    • 0028022882 scopus 로고
    • Microtubule associated protein MAP1A is an actin-binding and cross-linking protein
    • Pedrotti, B., Colombo, R., and Islam, K. (1994). Microtubule associated protein MAP1A is an actin-binding and cross-linking protein. Cell Motil. Cytoskeleton 29, 110-116.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 110-116
    • Pedrotti, B.1    Colombo, R.2    Islam, K.3
  • 72
    • 0032571406 scopus 로고    scopus 로고
    • Protein kinase C-theta phosphorylation of moesin in the actin-binding sequence
    • Pietromonaco, S.F., Simons, P.C., Altman, A., and Elias, L. (1998). Protein kinase C-theta phosphorylation of moesin in the actin-binding sequence. J. Biol. Chem. 273, 7594-7603.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7594-7603
    • Pietromonaco, S.F.1    Simons, P.C.2    Altman, A.3    Elias, L.4
  • 73
    • 0026542434 scopus 로고
    • Structural changes in profilin accompany its binding to phosphatidylinositol 4,5-biphosphate
    • Ragunathan, V., Mowery, P., Rozycki, M., Lindberg, U., and Schutt, C. (1992). Structural changes in profilin accompany its binding to phosphatidylinositol 4,5-biphosphate. FEBS Lett. 297, 46-50.
    • (1992) FEBS Lett. , vol.297 , pp. 46-50
    • Ragunathan, V.1    Mowery, P.2    Rozycki, M.3    Lindberg, U.4    Schutt, C.5
  • 74
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • 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, 169-179.
    • (1997) J. Cell Biol. , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 75
    • 0030835761 scopus 로고    scopus 로고
    • A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding
    • Roy, C., Martin, M., and Mangeat, P. (1997). A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding. J. Biol. Chem. 272, 20088-20095.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20088-20095
    • Roy, C.1    Martin, M.2    Mangeat, P.3
  • 76
    • 0029658495 scopus 로고    scopus 로고
    • Rho is required for alphaq and alpha1-adrenergic receptor signaling in cardiomyocytes. Dissociation of Ras and Rho pathways
    • Sah, V.P., Hoshijima, M., Chien, K.R., and Brown, J.H. (1996). Rho is required for alphaq and alpha1-adrenergic receptor signaling in cardiomyocytes. Dissociation of Ras and Rho pathways. J. Biol. Chem. 271, 31185-31190.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31185-31190
    • Sah, V.P.1    Hoshijima, M.2    Chien, K.R.3    Brown, J.H.4
  • 77
    • 0020614164 scopus 로고
    • A role of calcium-activated phospholipid-dependent protein kinase in human platelet activation. Comparison of thrombin and collagen actions
    • Sano, K., Takai, Y., Yamanishi, J., and Nishizuka, Y. (1983). A role of calcium-activated phospholipid-dependent protein kinase in human platelet activation. Comparison of thrombin and collagen actions. J. Biol. Chem. 258, 2010-2013.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2010-2013
    • Sano, K.1    Takai, Y.2    Yamanishi, J.3    Nishizuka, Y.4
  • 78
    • 0028588079 scopus 로고
    • Tyrosine kinases regulate the cytoskeletal attachment of integrin alpha IIb beta 3 (platelet glycoprotein Ilb/IIIa) and the cellular retraction of fibrin polymers
    • Schoenwaelder, S.M., Jackson, S.P., Yuan, Y., Teasdale, M.S., Salem, H.H., and Mitchell, C.A. (1994). Tyrosine kinases regulate the cytoskeletal attachment of integrin alpha IIb beta 3 (platelet glycoprotein Ilb/IIIa) and the cellular retraction of fibrin polymers. J. Biol. Chem. 269, 32479-32487.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32479-32487
    • Schoenwaelder, S.M.1    Jackson, S.P.2    Yuan, Y.3    Teasdale, M.S.4    Salem, H.H.5    Mitchell, C.A.6
  • 79
    • 0030847406 scopus 로고    scopus 로고
    • Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T-lymphocytes during cell polarization
    • 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, 1409-1423.
    • (1997) J. Cell Biol. , vol.138 , pp. 1409-1423
    • Serrador, J.M.1    Alonso-Lebrero, J.L.2    Del Pozo, M.A.3    Furthmayr, H.4    Schwartz-Albiez, R.5    Calvo, J.6    Lozano, F.7    Sanchez-Madrid, F.8
  • 80
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R.J., Henry, M., Solomon, F., and Jacks, T. (1998). RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell 9, 403-419.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 82
    • 0032583447 scopus 로고    scopus 로고
    • C-terminal threonine phosphorylation activates ERM proteins to link the cells' cortical lipid bilayer
    • Simons, P.C., Pietromonaco, S.F., Reczek, D., Bretscher, A., and Elias, L. (1998). C-terminal threonine phosphorylation activates ERM proteins to link the cells' cortical lipid bilayer. Biochem. Biophys. Res. Commun. 253, 561-565.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 561-565
    • Simons, P.C.1    Pietromonaco, S.F.2    Reczek, D.3    Bretscher, A.4    Elias, L.5
  • 83
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A., and Watt, S. (1971). The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 84
    • 0023858663 scopus 로고
    • Solubilization, purification, and characterization of an inositol triphosphate receptor
    • Supattopone, S., Worley, P.F., Baraban, J.M., and Snyder, S.H. (1988). Solubilization, purification, and characterization of an inositol triphosphate receptor. J. Biol. Chem. 263, 1530-1534.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1530-1534
    • Supattopone, S.1    Worley, P.F.2    Baraban, J.M.3    Snyder, S.H.4
  • 85
    • 0029615381 scopus 로고
    • 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
    • Takeda, H., Nagafuchi, A., Yonemura, S., Tsukita, S., Behrens, J., Birchmeier, W., and Tsukita, S. (1995). 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. 131, 1839-1847.
    • (1995) J. Cell Biol. , vol.131 , pp. 1839-1847
    • Takeda, H.1    Nagafuchi, A.2    Yonemura, S.3    Tsukita, S.4    Behrens, J.5    Birchmeier, W.6    Tsukita, S.7
  • 86
  • 87
    • 0017072431 scopus 로고
    • Cytidine diphosphate diglyceride of bovine brain. Positional distribution of fatty acids and analysis of major molecular species
    • Thompson, W., and MacDonald, G. (1976). Cytidine diphosphate diglyceride of bovine brain. Positional distribution of fatty acids and analysis of major molecular species. Eur. J. Biochem. 65, 107-111.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 107-111
    • Thompson, W.1    MacDonald, G.2
  • 89
    • 0024320199 scopus 로고
    • A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: Purification and characterization
    • Tsukita, S., Hieda, Y., and Tsukita, S. (1989). A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization. J. Cell Biol. 108, 2369-2382.
    • (1989) J. Cell Biol. , vol.108 , pp. 2369-2382
    • Tsukita, S.1    Hieda, Y.2    Tsukita, S.3
  • 90
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • 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, 1445-1453.
    • (1994) J. Cell Biol. , vol.126 , pp. 1445-1453
    • Turunen, O.1    Wahlstrom, T.2    Vaheri, A.3
  • 91
    • 0024338942 scopus 로고
    • Characterization of an 80-kDA phosphoprotein involved in parietal cell stimulation
    • Urushidani, T., Hanzel, D.K., and Forte, J.G. (1989). Characterization of an 80-kDA phosphoprotein involved in parietal cell stimulation. Am. J. Physiol. 256, 1070-1081.
    • (1989) Am. J. Physiol. , vol.256 , pp. 1070-1081
    • Urushidani, T.1    Hanzel, D.K.2    Forte, J.G.3
  • 92
    • 0029862987 scopus 로고    scopus 로고
    • Biochemical characterization of ezrin-actin interaction
    • Yao, X., Cheng, L., and Forte, J.G. (1996). Biochemical characterization of ezrin-actin interaction. J. Biol. Chem. 271, 7224-7229.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7224-7229
    • Yao, X.1    Cheng, L.2    Forte, J.G.3
  • 93
    • 0027509048 scopus 로고
    • Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons
    • Yonemura, S., Nagafuchi, A., Sato, N., and Tsukita, S. (1993). Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons. J. Cell Biol. 120, 437-449.
    • (1993) J. Cell Biol. , vol.120 , pp. 437-449
    • Yonemura, S.1    Nagafuchi, A.2    Sato, N.3    Tsukita, S.4
  • 94
    • 0027374497 scopus 로고
    • Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho
    • Zhang, J., King, W.G., Dillon, S., Hall, A., Feig, L., and Rittenhouse, S.E. (1993). Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho. J. Biol. Chem. 268, 22251-22254.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22251-22254
    • Zhang, J.1    King, W.G.2    Dillon, S.3    Hall, A.4    Feig, L.5    Rittenhouse, S.E.6
  • 95
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through rho-dependent actin stress fiber formation and cell contraction
    • Zhang, Q., Magnusson, M.K., and Mosher, D.F. (1997). Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through rho-dependent actin stress fiber formation and cell contraction. Mol. Biol. Cell 8, 1415-1425.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.K.2    Mosher, D.F.3


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