메뉴 건너뛰기




Volumn 147, Issue 7, 1999, Pages 1533-1547

Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium

Author keywords

Antisense; Cortical cytoskeleton; Epithelia; Ezrin radixin moesin proteins; Retinal development

Indexed keywords

COMPLEMENTARY DNA; EZRIN; MOESIN; RADIXIN;

EID: 0033611058     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.7.1533     Document Type: Article
Times cited : (136)

References (63)
  • 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. 120:129-139.
    • (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
    • 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., P. Litman, L. Huang, E. Ichimaru, and H. Furthmayr. 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. 112:111-125.
    • (1998) J. Cell Sci. , vol.112 , pp. 111-125
    • Amieva, M.R.1    Litman, P.2    Huang, L.3    Ichimaru, E.4    Furthmayr, H.5
  • 3
    • 0028048235 scopus 로고
    • Ezrin has properties to self-associate at the plasma membrane
    • Andreoli, C., M. Martin, R. Le Borgne, H. Reggio, and P. Mangeat. 1994. Ezrin has properties to self-associate at the plasma membrane. J. Cell Sci. 107: 2509-2521.
    • (1994) J. Cell Sci. , vol.107 , pp. 2509-2521
    • Andreoli, C.1    Martin, M.2    Le Borgne, R.3    Reggio, H.4    Mangeat, P.5
  • 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
    • 0029131685 scopus 로고
    • Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation
    • Barila, D., C. Murgia, F. Nobili, and G. Perozzi. 1995. Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation. Biochim. Biophys. Acta. 1263:133-140.
    • (1995) Biochim. Biophys. Acta. , vol.1263 , pp. 133-140
    • Barila, D.1    Murgia, C.2    Nobili, F.3    Perozzi, G.4
  • 6
    • 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
  • 7
    • 0027741818 scopus 로고
    • The retinal pigment epithelium, a versatile partner in vision
    • Bok, D. 1993. The retinal pigment epithelium, a versatile partner in vision. J. Cell Sci. 17:189-195.
    • (1993) J. Cell Sci. , vol.17 , pp. 189-195
    • Bok, D.1
  • 8
    • 0030755820 scopus 로고    scopus 로고
    • Apical sorting of hemagluttinin by transcytosis in retinal pigment epithelium
    • Bonilha, V.L., A.D. Marmorstein, L. Cohen-Gould, and E. Rodriguez-Boulan. 1997. Apical sorting of hemagluttinin by transcytosis in retinal pigment epithelium. J. Cell Sci. 110:1717-1727.
    • (1997) J. Cell Sci. , vol.110 , pp. 1717-1727
    • Bonilha, V.L.1    Marmorstein, A.D.2    Cohen-Gould, L.3    Rodriguez-Boulan, E.4
  • 9
    • 0014713173 scopus 로고
    • Development of the retinal pigment epithelium, choriocapillaris and Bruch's membrane in the albino rat
    • Braekevelt, C.R., and M.J. Hollenberg. 1970. Development of the retinal pigment epithelium, choriocapillaris and Bruch's membrane in the albino rat. Exp. Eye Res. 9:124-131.
    • (1970) Exp. Eye Res. , vol.9 , pp. 124-131
    • Braekevelt, C.R.1    Hollenberg, M.J.2
  • 10
    • 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
  • 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
    • 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
  • 13
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C.A., and H. Okayama. 1988. Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. Biotechniques. 6:632-638.
    • (1988) Biotechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 15
    • 0028821179 scopus 로고
    • Suppression of villin expression by antisense RNA impairs brush border assembly in polarized epithelial intestinal cells
    • Costa de Beauregard, M.A., E. Pringault, S. Robine, and D. Louvard. 1995. Suppression of villin expression by antisense RNA impairs brush border assembly in polarized epithelial intestinal cells. EMBO (Eur. Mol. Biol. Organ.) J. 14:409-421.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 409-421
    • Costa De Beauregard, M.A.1    Pringault, E.2    Robine, S.3    Louvard, D.4
  • 16
    • 0030763919 scopus 로고    scopus 로고
    • Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
    • Crepaldi, T., A. Gautreau, P.M. Comoglio, D. Louvard, and M. Arpin. 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
  • 17
    • 0028903353 scopus 로고
    • A human retinal pigment epithelial cell line that retains epithelial characteristics after prolonged culture
    • Davis, A.A., P.S. Bernstein, D. Bok, J. Turner, M. Nachtigal, and R.C. Hunt. 1995. A human retinal pigment epithelial cell line that retains epithelial characteristics after prolonged culture. Invest. Ophthalmol. Vis. Sci. 36:955-964.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 955-964
    • Davis, A.A.1    Bernstein, P.S.2    Bok, D.3    Turner, J.4    Nachtigal, M.5    Hunt, R.C.6
  • 18
    • 0033593481 scopus 로고    scopus 로고
    • Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout
    • Doi, Y., M. Itoh, S. Yonemura, S. Ishihara, H. Takano, T. Noda, Sh. Tsukita, and Sa. Tsukita. 1999. Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout. J. Biol. Chem. 274: 2315-2321.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2315-2321
    • Doi, Y.1    Itoh, M.2    Yonemura, S.3    Ishihara, S.4    Takano, H.5    Noda, T.6    Tsukita, Sh.7    Tsukita, Sa.8
  • 20
    • 0021893222 scopus 로고
    • Relation of retinomotor responses and contractile proteins in vertebrate retinas
    • Drenckhahn, D., and H.J. Wagner. 1985. Relation of retinomotor responses and contractile proteins in vertebrate retinas. Eur. J. Cell Biol. 37:156-168.
    • (1985) Eur. J. Cell Biol. , vol.37 , pp. 156-168
    • Drenckhahn, D.1    Wagner, H.J.2
  • 21
    • 0030695436 scopus 로고    scopus 로고
    • Phagocytosis of rod outer segments by retinal pigment epithelial cells requires αvβ5 integrin for binding but not for internalization
    • Finnemann, S.C., V.L. Bonilha, A.D. Marmorstein, and E. Rodriguez-Boulan. 1997. Phagocytosis of rod outer segments by retinal pigment epithelial cells requires αvβ5 integrin for binding but not for internalization. Proc. Natl. Acad. Sci. USA. 94:12932-12937.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12932-12937
    • Finnemann, S.C.1    Bonilha, V.L.2    Marmorstein, A.D.3    Rodriguez-Boulan, E.4
  • 22
    • 0024317269 scopus 로고
    • Villin induces microvilli growth and actin redistribution in transfected fibroblasts
    • Friederich, E., C. Huet, M. Arpin, and D. Louvard. 1989. Villin induces microvilli growth and actin redistribution in transfected fibroblasts. Cell. 59: 461-475.
    • (1989) Cell , vol.59 , pp. 461-475
    • Friederich, E.1    Huet, C.2    Arpin, M.3    Louvard, D.4
  • 24
    • 0032425542 scopus 로고    scopus 로고
    • Janus kinases and focal adhesion kinases play in the 4.1 band: A superfamily of band 4.1 domains important for cell structure and signal transduction
    • Girault, J.A., G. Labesse, J.P. Mornon, and I. Callebaut. 1998. Janus kinases and focal adhesion kinases play in the 4.1 band: A superfamily of band 4.1 domains important for cell structure and signal transduction. Mol. Med. 4:751-769.
    • (1998) Mol. Med. , vol.4 , pp. 751-769
    • Girault, J.A.1    Labesse, G.2    Mornon, J.P.3    Callebaut, I.4
  • 25
    • 0027529492 scopus 로고
    • Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina
    • Gundersen, D., S.K. Powell, and E. Rodriguez-Boulan. 1993. Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina. J. Cell Biol. 121:335-343.
    • (1993) J. Cell Biol. , vol.121 , pp. 335-343
    • Gundersen, D.1    Powell, S.K.2    Rodriguez-Boulan, E.3
  • 26
    • 0025769919 scopus 로고
    • The secretion-stimulated 80K phosphoprotein of parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli
    • published erratum appears in EMBO (Eur. Mol. Biol. Organ.) J. 1991. 10:3978-3981
    • Hanzel, D., H. Reggio, A. Bretscher, J.G. Forte, and P. Mangeat. 1991. The secretion-stimulated 80K phosphoprotein of 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. [published erratum appears in EMBO (Eur. Mol. Biol. Organ.) J. 1991. 10:3978-3981].
    • (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
    • 0029163054 scopus 로고
    • Molecular motors, membrane movements and physiology: Emerging roles for myosins
    • Hasson, T., and M.S. Mooseker. 1995. Molecular motors, membrane movements and physiology: emerging roles for myosins. Curr. Opin. Cell Biol. 7:587-594.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 587-594
    • Hasson, T.1    Mooseker, M.S.2
  • 28
    • 0029033133 scopus 로고
    • Molecular dissection of radixin: Distinct and interdependent functions of the amino- And carboxyterminal domains
    • Henry, M.D., C. Gonzalez Agosti, and F. Solomon. 1995. Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxyterminal 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
  • 29
    • 0023388436 scopus 로고
    • Characterization of retinal pigment epithelial cells cultured on microporous filters
    • Heth, C.A., M.A. Yankauckas, M. Adamian, and R.B. Edwards. 1987. Characterization of retinal pigment epithelial cells cultured on microporous filters. Curr. Eye Res. 6:1007-1019.
    • (1987) Curr. Eye Res. , vol.6 , pp. 1007-1019
    • Heth, C.A.1    Yankauckas, M.A.2    Adamian, M.3    Edwards, R.B.4
  • 30
    • 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., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, Sh. Tsukita, and Sa. Tsukita. 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. 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
  • 31
    • 0027477699 scopus 로고
    • Molecular heterogeneity of the actin filament cytoskeleton associated with microvilli of photoreceptors, muller glial cells and pigment epithelial cells of the retina
    • Hofer, D., and D. Drenckhahn. 1993. Molecular heterogeneity of the actin filament cytoskeleton associated with microvilli of photoreceptors, muller glial cells and pigment epithelial cells of the retina. Histochemistry. 99:29-35.
    • (1993) Histochemistry , vol.99 , pp. 29-35
    • Hofer, D.1    Drenckhahn, D.2
  • 32
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T.E. 1986. Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO (Eur. Mol. Biol. Organ.) J. 5:931-941.
    • (1986) EMBO (Eur. Mol. Biol. Organ.) J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 33
    • 0023403268 scopus 로고
    • Microtubules containing detyrosinated tubulin are less dynamic
    • Kreis, T.E. 1987. Microtubules containing detyrosinated tubulin are less dynamic. EMBO (Eur. Mol. Biol. Organ.) J. 6:2597-2606.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 2597-2606
    • Kreis, T.E.1
  • 34
    • 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., B.W. Ozanne, C. Roy, L. McGarry, C. Stipp, P. Mangeat, and D.G. Jay. 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
  • 35
    • 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
  • 36
    • 0030811605 scopus 로고    scopus 로고
    • Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells
    • Liu, X., G. Vansant, I.P. Udovichenko, U. Wolfrum, and D.S. Williams. 1997. Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells. Cell Motil. Cytoskelet. 37:240-252.
    • (1997) Cell Motil. Cytoskelet , vol.37 , pp. 240-252
    • Liu, X.1    Vansant, G.2    Udovichenko, I.P.3    Wolfrum, U.4    Williams, D.S.5
  • 37
    • 0032940071 scopus 로고    scopus 로고
    • ERM proteins in cell adhesion and membrane dynamics
    • Mangeat, P., C. Roy, and M. Martin. 1999. ERM proteins in cell adhesion and membrane dynamics. Trends Cell Biol. 9:187-192.
    • (1999) Trends Cell Biol. , vol.9 , pp. 187-192
    • Mangeat, P.1    Roy, C.2    Martin, M.3
  • 38
    • 0031877495 scopus 로고    scopus 로고
    • Apical polarity of N-CAM and EMMPRin in retinal pigment epithelium resulting from suppression of basolateral signal recognition
    • Marmorstein, A.D., Y.C. Gan, V.L. Bonilha, S.C. Finnemann, K.G. Csaky, and E. Rodriguez-Boulan. 1998. Apical polarity of N-CAM and EMMPRIN in retinal pigment epithelium resulting from suppression of basolateral signal recognition. J. Cell Biol. 142:697-710.
    • (1998) J. Cell Biol. , vol.142 , pp. 697-710
    • Marmorstein, A.D.1    Gan, Y.C.2    Bonilha, V.L.3    Finnemann, S.C.4    Csaky, K.G.5    Rodriguez-Boulan, E.6
  • 40
    • 0030883688 scopus 로고    scopus 로고
    • Three determinants in ezrin are responsible for cell extension activity
    • Martin, M., C. Roy, P. Montcourrier, A. Sahuquet, and P. Mangeat. 1997. Three determinants in ezrin are responsible for cell extension activity. Mol. Biol. Cell. 8:1543-1557.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1543-1557
    • Martin, M.1    Roy, C.2    Montcourrier, P.3    Sahuquet, A.4    Mangeat, P.5
  • 41
    • 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., M. Maeda, Y. Doi, S. Yonemura, M. Amano, K. Kaibuchi, Sa. Tsukita, and Sh. Tsukita. 1998. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140:647-557.
    • (1998) J. Cell Biol. , vol.140 , pp. 647-1557
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, Sh.7    Tsukita, Sa.8
  • 43
    • 0022416552 scopus 로고
    • Increase in actin contents and elongation of apical projections in retinal pigmented epithelial cells during development of the chicken eye
    • Owaribe, K., and G. Eguchi. 1985. Increase in actin contents and elongation of apical projections in retinal pigmented epithelial cells during development of the chicken eye. J. Cell Biol. 101:590-596.
    • (1985) J. Cell Biol. , vol.101 , pp. 590-596
    • Owaribe, K.1    Eguchi, G.2
  • 44
    • 0032547839 scopus 로고    scopus 로고
    • Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons
    • Paglini, G., P. Kunda, S. Quiroga, K. Kosik, and A. Caceres. 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    Caceres, A.5
  • 46
    • 0032571406 scopus 로고    scopus 로고
    • Protein kinase C-theta phosphorylation of moesin in the actin-binding sequence
    • Pietromonaco, S.F., P.C. Simons, A. Altman, and L. Elias. 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
  • 47
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • Reczek, D., M. Berryman, and A. Bretscher. 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
  • 48
    • 0030835761 scopus 로고    scopus 로고
    • A dual involvement of the amino-terminal domain of ezrin in F- And G-actin binding
    • Roy, C., M. Martin, and P. Mangeat. 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
  • 49
    • 0029116771 scopus 로고
    • Differential expression of the microspike-associated protein moesin in human tissues
    • Schwartz-Albiez, R., A. Merling, H. Spring, P. Moller, and K. Koretz. 1995. Differential expression of the microspike-associated protein moesin in human tissues. Eur. J. Cell Biol. 67:189-198.
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 189-198
    • Schwartz-Albiez, R.1    Merling, A.2    Spring, H.3    Moller, P.4    Koretz, K.5
  • 50
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R.J., M. Henry, F. Solomon, and T. Jacks, 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
  • 51
    • 0032583447 scopus 로고    scopus 로고
    • C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton
    • Simons, P.C., S.F. Pietromonaco, D. Reczek, A. Bretscher, and L. Elias. 1998. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton. Biochem. Biophys. Res. Commun. 253:561-565.
    • (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
  • 53
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi, K., T. Sasaki, A. Mammoto, K. Takaishi, T. Kameyama, Sa. Tsukita, Sh. Tsukita, and Y. Takai. 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. 272:23371-23375.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, Sa.6    Tsukita, Sh.7    Takai, Y.8
  • 55
    • 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. 1989a. 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, Sa.1    Hieda, Y.2    Tsukita, Sh.3
  • 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, and A. Kawai. 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
  • 57
    • 0024785788 scopus 로고
    • A new 400-kD protein from isolated adherens junction: Its localization at the undercoat of adherens junctions and at microfilament bundles such as stress fibers and circumferential bundles
    • Tsukita, Sh., M. Itoh, and Sa. Tsukita. 1989b. A new 400-kD protein from isolated adherens junction: its localization at the undercoat of adherens junctions and at microfilament bundles such as stress fibers and circumferential bundles. J. Cell Biol. 109:2905-2915.
    • (1989) J. Cell Biol. , vol.109 , pp. 2905-2915
    • Tsukita, Sh.1    Itoh, M.2    Tsukita, Sa.3
  • 58
    • 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. 126:445-1453.
    • (1994) J. Cell Biol. , vol.126 , pp. 445-1453
    • Turunen, O.1    Wahlstrom, T.2    Vaheri, A.3
  • 59
    • 0023194180 scopus 로고
    • The distribution of F-actin in cells isolated from vertebrate retinas
    • Vaughan, D.K., and S.K. Fisher. 1987. The distribution of F-actin in cells isolated from vertebrate retinas. Exp. Eye Res. 44:393-406.
    • (1987) Exp. Eye Res. , vol.44 , pp. 393-406
    • Vaughan, D.K.1    Fisher, S.K.2
  • 60
    • 0027162182 scopus 로고
    • Ezrin-calpain I interactions in gastric parietal cells
    • Yao, X., A. Thibodeau, and J.G. Forte. 1993. Ezrin-calpain I interactions in gastric parietal cells. Am J. Physiol. 265:C36-C46.
    • (1993) Am J. Physiol. , vol.265
    • Yao, X.1    Thibodeau, A.2    Forte, J.G.3
  • 61
    • 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
  • 62
    • 0033612533 scopus 로고    scopus 로고
    • Direct involvement of ezrin/ radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins
    • Yonemura, S., Sa. Tsukita, and Sh. Tsukita. 1999. Direct involvement of ezrin/ radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J. Cell Biol. 145: 1497-1509.
    • (1999) J. Cell Biol. , vol.145 , pp. 1497-1509
    • Yonemura, S.1    Tsukita, Sa.2    Tsukita, Sh.3
  • 63
    • 0002441838 scopus 로고
    • Anatomy of the human retinal pigment epithelium
    • K.M. Zinn and M.F. Marmor, editors. Harvard University Press, Cambridge, MA.
    • Zinn, K.M., and J.V. Benjamin-Henkind. 1979. Anatomy of the human retinal pigment epithelium. In The Retinal Pigment Epithelium. K.M. Zinn and M.F. Marmor, editors. Harvard University Press, Cambridge, MA. 3-31.
    • (1979) The Retinal Pigment Epithelium , pp. 3-31
    • Zinn, K.M.1    Benjamin-Henkind, J.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.