메뉴 건너뛰기




Volumn 140, Issue 4, 1998, Pages 885-895

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

Author keywords

[No Author keywords available]

Indexed keywords

EZRIN; HERMES ANTIGEN; INTERCELLULAR ADHESION MOLECULE 2; LEUKOSIALIN; MOESIN; RADIXIN;

EID: 0032559637     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.4.885     Document Type: Article
Times cited : (517)

References (64)
  • 1
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain, M., O. Turunen, A. Vaheri, D. Louvard, and M. Arpin. 1993. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120:129-140.
    • (1993) J. Cell Biol. , vol.120 , pp. 129-140
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 2
    • 0028206028 scopus 로고
    • Radixin is a component of hepatocyte microvilli in situ
    • Amieva, M.R., K.K. Wilgenbuns, and H. Furthmayr. 1994. Radixin is a component of hepatocyte microvilli in situ. Exp. Cell Res. 210:140-144.
    • (1994) Exp. Cell Res. , vol.210 , pp. 140-144
    • Amieva, M.R.1    Wilgenbuns, K.K.2    Furthmayr, H.3
  • 4
    • 0028013757 scopus 로고
    • Membrane-actin microfilament connections: An increasing diversity of players related to band 4.1
    • Arpin, M., M. Algrain, and D. Louvard. 1994. Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1. Curr. Opin. Cell Biol. 6:136-141.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 136-141
    • Arpin, M.1    Algrain, M.2    Louvard, D.3
  • 5
    • 0024552276 scopus 로고
    • The spectrin-actin junction of erythrocyte membrane skeletons
    • Bennett, V. 1989. The spectrin-actin junction of erythrocyte membrane skeletons. Biochem. Biophys. Acta. 988:107-121.
    • (1989) Biochem. Biophys. Acta , vol.988 , pp. 107-121
    • Bennett, V.1
  • 7
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells, whereas moesin is found primarily in endothelial cells
    • Berryman, M., Z. Franck, and A. Bretscher. 1993. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells, whereas moesin is found primarily in endothelial cells. J. Cell Sci. 105:1025-1043.
    • (1993) J. Cell Sci. , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 8
    • 0028821843 scopus 로고
    • Ezrin oligomers are major cytoskeletal components of placental microvilli: A proposal for their involvement in cortical morphogenesis
    • Berryman, M., R. Gary, and A. Bretscher. 1995. Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis. J. Cell Biol. 131:1231-1242.
    • (1995) J. Cell Biol. , vol.131 , pp. 1231-1242
    • Berryman, M.1    Gary, R.2    Bretscher, A.3
  • 9
    • 0025059797 scopus 로고
    • The role of charged amino acids in the localization of secreted and membrane proteins
    • Boyde, D., and J. Beckwith. 1990. The role of charged amino acids in the localization of secreted and membrane proteins. Cell. 62:1031-1033.
    • (1990) Cell , vol.62 , pp. 1031-1033
    • Boyde, D.1    Beckwith, J.2
  • 10
    • 0020804117 scopus 로고
    • Purification of an 80,000-dalton protein that is a component of isolated microvillus cytoskeleton, and its localization in nonmuscle cells
    • Bretscher, A. 1983. Purification of an 80,000-dalton protein that is a component of isolated microvillus cytoskeleton, and its localization in nonmuscle cells. J. Cell Biol. 97:425-432.
    • (1983) J. Cell Biol. , vol.97 , pp. 425-432
    • Bretscher, A.1
  • 11
    • 0024542907 scopus 로고
    • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
    • Bretscher, A. 1989. Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J. Cell Biol. 108:921-930.
    • (1989) J. Cell Biol. , vol.108 , pp. 921-930
    • Bretscher, A.1
  • 12
    • 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., R. Gary, and M. Berryman. 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
  • 13
    • 0026672861 scopus 로고
    • Association of intercellular adhesion molecule-1 (ICAM-1) with aclin-containina cytoskeleton and α-actinin
    • Carpén, O., P. Pallai, D.E. Staunton, and T.A. Springer. 1992. Association of intercellular adhesion molecule-1 (ICAM-1) with aclin-containina cytoskeleton and α-actinin. J. Cell Biol. 118:1223-1234.
    • (1992) J. Cell Biol. , vol.118 , pp. 1223-1234
    • Carpén, O.1    Pallai, P.2    Staunton, D.E.3    Springer, T.A.4
  • 14
    • 0029084127 scopus 로고
    • Dephospohrylation of ezrin as an early event in renal microvillar breakdown and anoxic injury
    • Chen, J., J.A. Cohn, and L.J. Mandel. 1995. Dephospohrylation 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
  • 15
    • 0011727270 scopus 로고
    • Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton
    • Conboy, J., Y.W. Kan, S.B. Shohet, and N. Mohandas. 1986. Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. Proc. Natl. Acad. Sci. USA. 83:9512-9516.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9512-9516
    • Conboy, J.1    Kan, Y.W.2    Shohet, S.B.3    Mohandas, N.4
  • 17
    • 84963072411 scopus 로고
    • Production of malignancy in vitro.IV. The mouse fibroblast cultures and changes seen in the living cells
    • Earl, W.R. 1943. Production of malignancy in vitro.IV. The mouse fibroblast cultures and changes seen in the living cells. J. Natl. Cancer Inst. 4:165-212.
    • (1943) J. Natl. Cancer Inst. , vol.4 , pp. 165-212
    • Earl, W.R.1
  • 19
    • 0027275994 scopus 로고
    • Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable
    • Franck, Z., R. Gary, and A. Bretscher. 1993. Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. J. Cell Sci. 105:219-231.
    • (1993) J. Cell Sci. , vol.105 , pp. 219-231
    • Franck, Z.1    Gary, R.2    Bretscher, A.3
  • 20
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni, J.V., and B.G. Nell. 1993. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 210:179-187.
    • (1993) Anal. Biochem. , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Nell, B.G.2
  • 22
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse, M., M. Itoh, T. Hirase, A. Nagafuchi, S. Yonemura, Sa. Tsukita, and Sh. Tsukita. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127: 1617-1626.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, Sa.6    Tsukita, Sh.7
  • 23
    • 0027364004 scopus 로고
    • Heterotypic and homotypic association between ezrin and moesin, two putative membrane-cytoskeletal linking proteins
    • Gary, R., and A. Bretscher. 1993. Heterotypic and homotypic association between ezrin and moesin, two putative membrane-cytoskeletal linking proteins. Proc. Natl. Acad. Sci. USA. 90:10846-10850.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10846-10850
    • Gary, R.1    Bretscher, A.2
  • 24
    • 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 A. Bretscher. 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
  • 25
    • 0024814175 scopus 로고
    • cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1
    • Gould, K.L., A. Bretscher, F.S. Esch, and T. Hunter. 1989. cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1 EMBO (Eur. Mol. Biol. Organ.) J. 8:4133-4142.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 4133-4142
    • Gould, K.L.1    Bretscher, A.2    Esch, F.S.3    Hunter, T.4
  • 26
    • 0025769919 scopus 로고
    • The secretion-stimulated 80K phosphoprotein of a parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli
    • Hanzel, D., H. Reggio, A. Bretscher, J.G. Forte, and P. Mangeat. 1991. The secretion-stimulated 80K phosphoprotein of a parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli. EMBO (Eur. Mol. Biol. Organ.) J. 10:2363-2373.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 2363-2373
    • Hanzel, D.1    Reggio, H.2    Bretscher, A.3    Forte, J.G.4    Mangeat, P.5
  • 27
    • 0027048901 scopus 로고
    • Molecular isoforms of murine CD44 and evidence that the membrane proximal domain is not critical for hyaluronate recognition
    • He, O., J. Lesley, R. Hyman, K. Ishihara, and P.W. Kincade. 1992. Molecular isoforms of murine CD44 and evidence that the membrane proximal domain is not critical for hyaluronate recognition. J. Cell Biol. 119:1711-1719.
    • (1992) J. Cell Biol. , vol.119 , pp. 1711-1719
    • He, O.1    Lesley, J.2    Hyman, R.3    Ishihara, K.4    Kincade, P.W.5
  • 29
    • 0029033133 scopus 로고
    • Molecular dissection of radixin: Distinct and interdependent functions of the amino- and carhoxyl-terminal domains
    • Henry, M.D., C. Gonzalez Agosti, and F. Solomon. 1995. Molecular dissection of radixin: distinct and interdependent functions of the amino-and carhoxyl-terminal domains. J. Cell Biol. 129:1007-1022.
    • (1995) J. Cell Biol. , vol.129 , pp. 1007-1022
    • Henry, M.D.1    Gonzalez Agosti, C.2    Solomon, F.3
  • 30
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM protein/ plasma membrane association: Possible involvement of phosphatidylinositol turnover and rho-dependent signaling pathway
    • Hirao, M., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, Sh. Tsukita, and Sa. Tsukita. 1996. Regulation mechanism of ERM protein/ plasma membrane association: possible involvement of phosphatidylinositol turnover and rho-dependent signaling pathway. J. Cell Biol. 135:37-52.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-52
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, Sh.8    Tsukita, Sa.9
  • 31
    • 0023661344 scopus 로고
    • The sequence of rat leukosialin (W3/13 antigen) reveals a molecule with O-linked glycosylation of one third of its extracellular amino acids
    • Killeen. N., A.N. Barclay, A.C. Willis, and A.F. Williams. 1987. The sequence of rat leukosialin (W3/13 antigen) reveals a molecule with O-linked glycosylation of one third of its extracellular amino acids. EMBO (Eur. Mol. Biol. Organ.) J. 6:4029-4034.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 4029-4034
    • Killeen, N.1    Barclay, A.N.2    Willis, A.C.3    Williams, A.F.4
  • 32
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-talin-ezrin family of proteins
    • Lankes, W., and H. Furthmayr. 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.1    Furthmayr, H.2
  • 33
    • 0023952245 scopus 로고
    • A heparin-hinding protein involved in inhibition of smooth-muscle cell proliferation
    • Lankes, W., A. Griesmacher, J. Grunwald, R. Schwarts-Albiez, and R. Keller. 1988. A heparin-hinding protein involved in inhibition of smooth-muscle cell proliferation. Biochem. J. 251:831-842.
    • (1988) Biochem. J. , vol.251 , pp. 831-842
    • Lankes, W.1    Griesmacher, A.2    Grunwald, J.3    Schwarts-Albiez, R.4    Keller, R.5
  • 34
    • 0030872949 scopus 로고    scopus 로고
    • Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay, D.J.G., F. Esch, H. Furthmayr, and A. Hall. 1997. Rho-and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin 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
  • 37
    • 0023225108 scopus 로고
    • Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA
    • Nagafuchi, A., Y. Shirayoshi, K. Okazaki, K. Yasuda, and M. Takeichi. 1987. Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA. Nature. 329:341-343.
    • (1987) Nature , vol.329 , pp. 341-343
    • Nagafuchi, A.1    Shirayoshi, Y.2    Okazaki, K.3    Yasuda, K.4    Takeichi, M.5
  • 38
    • 0029569120 scopus 로고
    • Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets
    • Nakamura, F., M.R. Amieva, and H. Furthmayr. 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
  • 39
    • 0029959840 scopus 로고    scopus 로고
    • Immunolocalizalion of CD44 and ERM family in osteoblasts and osteoclasts in mouse tibiae
    • Nakamura, H., and H. Ozawa. 1996. Immunolocalizalion of CD44 and ERM family in osteoblasts and osteoclasts in mouse tibiae. J. Bone Miner. Res. 11: 1715-1722.
    • (1996) J. Bone Miner. Res. , vol.11 , pp. 1715-1722
    • Nakamura, H.1    Ozawa, H.2
  • 40
    • 0024295439 scopus 로고
    • Expressed recombinant cadherins mediate cell sorting in model systems
    • Nose, A., A. Nagafuchi, and M. Takeichi. 1988. Expressed recombinant cadherins mediate cell sorting in model systems. Cell. 54:993-1001.
    • (1988) Cell , vol.54 , pp. 993-1001
    • Nose, A.1    Nagafuchi, A.2    Takeichi, M.3
  • 41
    • 0023161676 scopus 로고
    • Microvillus-specific Mr 75,000 plasma membrane protein of human choriocarcinoma cells
    • Pakkanen, R., K. Hedman, O. Turunen, T. Wahlstrom, and A. Vaheri. 1987. Microvillus-specific Mr 75,000 plasma membrane protein of human choriocarcinoma cells. J. Histochem. Cytochem. 135:809-816.
    • (1987) J. Histochem. Cytochem. , vol.135 , pp. 809-816
    • Pakkanen, R.1    Hedman, K.2    Turunen, O.3    Wahlstrom, T.4    Vaheri, A.5
  • 42
    • 0029074732 scopus 로고
    • The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: Receptor positioning in microvilli does not require interaction with α-actinin
    • Pavalko, P.M., D.M. Walker, L. Graham, M. Goheen, C.M. Doerschuk, and G.S. Kansas. 1995. The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: receptor positioning in microvilli does not require interaction with α-actinin. J. Cell Biol. 129:1155-1164.
    • (1995) J. Cell Biol. , vol.129 , pp. 1155-1164
    • Pavalko, P.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 44
    • 0025939215 scopus 로고
    • The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular seleclins ELAM-1 and GMP-140
    • Picker, L.J., R.A. Warnock, A.R. Burns, C.M. Doerschuk, E.L. Berg, and E.C. Butcher. 1991. The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular seleclins ELAM-1 and GMP-140. Cell. 66:921-933.
    • (1991) Cell , vol.66 , pp. 921-933
    • Picker, L.J.1    Warnock, R.A.2    Burns, A.R.3    Doerschuk, C.M.4    Berg, E.L.5    Butcher, E.C.6
  • 45
    • 0024990759 scopus 로고
    • Sequence and domain structures of talin
    • Rees, D.J.G., S.E. Ades, S.J. Singer, and R.O. Hynes. 1990. Sequence and domain structures of talin. Nature. 347:685-689.
    • (1990) Nature , vol.347 , pp. 685-689
    • Rees, D.J.G.1    Ades, S.E.2    Singer, S.J.3    Hynes, R.O.4
  • 47
    • 0025736018 scopus 로고
    • Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis
    • Sato, N., S. Yonemura, T. Obinata, Sa. Tsukita, and Sh. Tsukita. 1991. Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis. J. Cell Biol. 113:321-330.
    • (1991) J. Cell Biol. , vol.113 , pp. 321-330
    • Sato, N.1    Yonemura, S.2    Obinata, T.3    Tsukita, Sa.4    Tsukita, Sh.5
  • 48
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin, and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato, N., N. Funayama, A. Nagafuchi, S. Yonemura, Sa. Tsukita, and Sh. Tsukita. 1992. A gene family consisting of ezrin, radixin, and moesin. Its specific localization at actin filament/plasma membrane association sites. J. Cell Sci. 103:131-143.
    • (1992) J. Cell Sci. , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, Sa.5    Tsukita, Sh.6
  • 49
    • 0022891682 scopus 로고
    • N-linked oligosaccharides are not involved in the function of a cell-cell binding glycoprotein E-cadherin
    • Shirayoshi, Y., A. Nose, K. Iwasaki, and M. Takeichi. 1986. N-linked oligosaccharides are not involved in the function of a cell-cell binding glycoprotein E-cadherin. Cell Struct. Funct. 11:245-252.
    • (1986) Cell Struct. Funct. , vol.11 , pp. 245-252
    • Shirayoshi, Y.1    Nose, A.2    Iwasaki, K.3    Takeichi, M.4
  • 50
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B., and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene (Amst.). 67:31-40.
    • (1988) Gene (Amst.) , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 51
  • 54
    • 0024320199 scopus 로고
    • A new 82 kD-barbed end capping protein (radixin) localized in the cell-to-cell adherens junction: Purification and characterization
    • Tsukita, Sa., Y. Hieda, and Sh. Tsukita. 1989. A new 82 kD-barbed end capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization. J. Cell Biol. 108:2356-2382.
    • (1989) J. Cell Biol. , vol.108 , pp. 2356-2382
    • Tsukita, Sa.1    Hieda, Y.2    Tsukita, Sh.3
  • 55
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-to-cell adherens junctions
    • Tsukita, Sh., Sa. Tsukita, A. Nagafuchi, and S. Yonemura. 1992. Molecular linkage between cadherins and actin filaments in cell-to-cell adherens junctions. Curr. Opin. Cell Biol. 4:834-839.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 834-839
    • Tsukita, Sh.1    Tsukita, Sa.2    Nagafuchi, A.3    Yonemura, S.4
  • 56
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita, Sa., K. Oishi, N. Sato, J. Sagara, A. Kawai, and Sh. Tsukita. 1994. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J. Cell Biol. 126:391-401.
    • (1994) J. Cell Biol. , vol.126 , pp. 391-401
    • Tsukita, Sa.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, Sh.6
  • 57
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita, Sa., S. Yonemura, and Sh. Tsukita. 1997a. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. (TIBS). 22:53-58.
    • (1997) Trends Biochem. Sci. (TIBS) , vol.22 , pp. 53-58
    • Tsukita, Sa.1    Yonemura, S.2    Tsukita, Sh.3
  • 58
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin) family: From cytoskeleton to signal transduction
    • Tsukita, Sa., S. Yonemura, and Sh. Tsukita. 1997b. ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9:70-75.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 70-75
    • Tsukita, Sa.1    Yonemura, S.2    Tsukita, Sh.3
  • 59
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • Turunen, O., T. Wahlstrom, and A. Vaheri. 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
  • 60
    • 0024474147 scopus 로고
    • Cytovillin, a microvillar Mr 75,000 protein, cDNa sequence, prokaryotic expression, and chromosomal localization
    • Turunen, O., R. Winqvist, R. Pakkane, K.H. Grzeschik, T. Wahlstrom, and A. Vaheri. 1989. Cytovillin, a microvillar Mr 75,000 protein, cDNA sequence, prokaryotic expression, and chromosomal localization. J. Biol. Chem. 264: 16727-16732.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16727-16732
    • Turunen, O.1    Winqvist, R.2    Pakkane, R.3    Grzeschik, K.H.4    Wahlstrom, T.5    Vaheri, A.6
  • 61
    • 0024338942 scopus 로고
    • Characterization of an 80-kDa phosphoprotein involved in parietal cell stimulation
    • Urushidani, T., D.K. Hanzel, and J.G. Forte. 1989. Characterization of an 80-kDa phosphoprotein involved in parietal cell stimulation. Am. J. Physiol. 256:G1070-G1081.
    • (1989) Am. J. Physiol. , vol.256
    • Urushidani, T.1    Hanzel, D.K.2    Forte, J.G.3
  • 62
    • 0029086105 scopus 로고
    • A central role for microvillous receptor presentation in leukocyte adhesion under flow
    • von Andrian, U.H., S.R. Hasslen, R.D. Nelson, S.L. Erlandsen, and E.C. Butcher. 1995. A central role for microvillous receptor presentation in leukocyte adhesion under flow. Cell. 82:989-999.
    • (1995) Cell , vol.82 , pp. 989-999
    • Von Andrian, U.H.1    Hasslen, S.R.2    Nelson, R.D.3    Erlandsen, S.L.4    Butcher, E.C.5
  • 63
    • 0026693787 scopus 로고
    • Isolation, characterization, and expression of mouse ICAM-2 complementary and genomic DNA
    • Xu, H., I.L. Tong, A.R. De Fougerolles, and T.A. Springer. 1992. Isolation, characterization, and expression of mouse ICAM-2 complementary and genomic DNA. J. Immunol. 149:2650-2655.
    • (1992) J. Immunol. , vol.149 , pp. 2650-2655
    • Xu, H.1    Tong, I.L.2    De Fougerolles, A.R.3    Springer, T.A.4
  • 64
    • 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., A. Nagafuchi, N. Sato, and Sh. Tsukita. 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. 120:37-449.
    • (1993) J. Cell Biol. , vol.120 , pp. 37-449
    • Yonemura, S.1    Nagafuchi, A.2    Sato, N.3    Tsukita, Sh.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.