메뉴 건너뛰기




Volumn 139, Issue 1, 1997, Pages 169-179

Identification of EPB50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family

Author keywords

[No Author keywords available]

Indexed keywords

EZRIN; MOESIN; PHOSPHOPROTEIN; RADIXIN; ACTIN BINDING PROTEIN; CARRIER PROTEIN; CYTOSKELETON PROTEIN; DLG1 PROTEIN, HUMAN; DLGH1 PROTEIN, MOUSE; DLGH4 PROTEIN, MOUSE; MEMBRANE PROTEIN; NERVE PROTEIN; PLASMA PROTEIN; POSTSYNAPTIC DENSITY PROTEINS; PROTEIN; RECOMBINANT PROTEIN; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SODIUM HYDROGEN EXCHANGER REGULATORY FACTOR; SODIUM PROTON EXCHANGE PROTEIN; SODIUM-HYDROGEN EXCHANGER REGULATORY FACTOR; ZONULA OCCLUDENS 1 PROTEIN; ZONULA OCCLUDENS-1 PROTEIN;

EID: 0030608877     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.1.169     Document Type: Article
Times cited : (522)

References (43)
  • 2
    • 0028206028 scopus 로고
    • Radixin is a component of hepatocyte microvilli in situ
    • Amieva, M.R., K.K. Wilgenbus, 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    Wilgenbus, K.K.2    Furthmayr, H.3
  • 3
    • 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
  • 4
    • 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
  • 5
    • 0020804117 scopus 로고
    • Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells
    • Bretscher, A. 1983. Purification of an 80,000-dalton protein that is a component of the 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
  • 6
    • 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
  • 7
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher, A. 1991. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7:337-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 8
    • 0018233556 scopus 로고
    • Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy
    • Bretscher, A., and K. Weber. 1978. Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy. J. Cell Biol. 79:839-845.
    • (1978) J. Cell Biol. , vol.79 , pp. 839-845
    • Bretscher, A.1    Weber, K.2
  • 11
    • 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
  • 13
    • 0027364004 scopus 로고
    • Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins
    • Gary, R., and A. Bretscher. 1993. Heterotypic and homotypic associations 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
  • 14
    • 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
    • Gay, 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
    • Gay, R.1    Bretscher, A.2
  • 15
    • 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
  • 16
    • 0029033133 scopus 로고
    • Molecular dissection of radixin: Distinct and interdependent functions of the amino- And carboxy-terminal domains
    • Henry, M.D., C.G. Agosti, and F. Solomon. 1995. Molecular dissection of radixin: distinct and interdependent functions of the amino-and carboxy-terminal domains. J. Cell Biol. 129:1007-1022.
    • (1995) J. Cell Biol. , vol.129 , pp. 1007-1022
    • Henry, M.D.1    Agosti, C.G.2    Solomon, F.3
  • 17
    • 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. 135:37-51.
    • (1996) J. Cell Biol. , vol.135 , 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, Sh.8    Tsukita, Sa.9
  • 19
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.-C., L.T. Schenker, M.B. Kennedy, and P.H. Seeburg. 1995. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science (Wash. DC). 269:1737-1740.
    • (1995) Science (Wash. DC) , vol.269 , pp. 1737-1740
    • Kornau, H.-C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-talin-ezrin family of proteins
    • Lankes, W.T., 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.T.1    Furthmayr, H.2
  • 23
    • 0028237630 scopus 로고
    • In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C
    • Marfatia, S.M., R.A. Lue, D. Branton, and A. Chisti. 1994. In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C. J. Biol. Chem. 269:8631-8634.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8631-8634
    • Marfatia, S.M.1    Lue, R.A.2    Branton, D.3    Chisti, A.4
  • 24
    • 0028917977 scopus 로고
    • Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor supressor protein
    • Marfatia, S.M., R.A. Lue, D. Branton, and A. Chisti. 1995. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor supressor protein. J. Biol. Chem. 270:715-719.
    • (1995) J. Biol. Chem. , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Lue, R.A.2    Branton, D.3    Chisti, A.4
  • 26
    • 0022172245 scopus 로고
    • Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border
    • Mooseker, M.S. 1985. Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Annu. Rev. Cell. Biol. 1:209-241.
    • (1985) Annu. Rev. Cell. Biol. , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 28
    • 0028800154 scopus 로고
    • Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin
    • Niggli, V., C. Andreoli, C. Roy, and P. Mangeat. 1995. Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS (Fed Eur. Biol. Soc.) Lett. 376:172-176.
    • (1995) FEBS (Fed Eur. Biol. Soc.) Lett. , vol.376 , pp. 172-176
    • Niggli, V.1    Andreoli, C.2    Roy, C.3    Mangeat, P.4
  • 29
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley, B., D. Kirsh, and N. Morris. 1980. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105:361-363.
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.1    Kirsh, D.2    Morris, N.3
  • 31
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • Ponting, C.P., and C. Phillips. 1995. DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biol. Sci. 20:102-103.
    • (1995) Trends Biol. Sci. , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 32
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras, J., and C.-H. Heldin. 1996. PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biol. Sci. 21:455-458.
    • (1996) Trends Biol. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.-H.2
  • 33
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin and moesin: Its specific localization and 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 and 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
  • 35
    • 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, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 36
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • Turunen, O., T. Wahlström, 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    Wahlström, T.2    Vaheri, A.3
  • 41
    • 0025858161 scopus 로고
    • Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase with homologuey to the cytoskeletal-associated proteins band 4.1, ezrin and talin
    • Yang, Q., and N.K. Tonks. 1991. Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase with homologuey to the cytoskeletal-associated proteins band 4.1, ezrin and talin. Proc. Natl. Acad. Sci. USA. 88:5949-5953.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5949-5953
    • Yang, Q.1    Tonks, N.K.2
  • 42
    • 0029862987 scopus 로고    scopus 로고
    • Biochemical characterization of ezrin-actin interaction
    • Yao, X., L. Cheng, and J.G. Forte. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.