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Ezrin Promotes Morphogenesis of Apical Microvilli and Basal Infoldings in Retinal Pigment Epithelium

Ezrin Promotes Morphogenesis of Apical Microvilli and Basal Infoldings in Retinal Pigment Epithelium Ezrin, a member of the ezrin/radixin/moesin (ERM) family, localizes to microvilli of epithelia in vivo, where it bridges actin filaments and plasma membrane proteins. Here, we demonstrate two specific morphogenetic roles of ezrin in the retinal pigment epithelium (RPE), i.e., the formation of very long apical microvilli and of elaborate basal infoldings typical of these cells, and characterize the role of ezrin in these processes using antisense and transfection approaches. In the adult rat RPE, only ezrin (no moesin or radixin) was detected at high levels by immunofluorescence and immunoelectron microscopy at microvilli and basal infoldings. At the time when these morphological differentiations develop, in the first two weeks after birth, ezrin levels increased fourfold to adult levels. Addition of ezrin antisense oligonucleotides to primary cultures of rat RPE drastically decreased both apical microvilli and basal infoldings. Transfection of ezrin cDNA into the RPE-J cell line, which has only trace amounts of ezrin and moesin, sparse and stubby apical microvilli, and no basal infoldings, induced maturation of microvilli and the formation of basal infoldings without changing moesin expression levels. Taken together, the results indicate that ezrin is a major determinant in the maturation of surface differentiations of RPE independently of other ERM family members. antisense retinal development cortical cytoskeleton epithelia ezrin radixin moesin proteins Footnotes Abbreviations used in this paper: ERM, ezrin/radixin/moesin family; HGF, hepatocyte growth factor; P, postnatal day; PR, photoreceptor; pAb, polyclonal antibody; RPE, retinal pigment epithelium; VSVG, vesicular stomatitis virus glycoprotein G. Submitted: 11 May 1999 Revision requested 17 November 1999 Accepted: 19 November 1999 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

Ezrin Promotes Morphogenesis of Apical Microvilli and Basal Infoldings in Retinal Pigment Epithelium

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Publisher
Rockefeller University Press
Copyright
© 1999 The Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.147.7.1533
Publisher site
See Article on Publisher Site

Abstract

Ezrin, a member of the ezrin/radixin/moesin (ERM) family, localizes to microvilli of epithelia in vivo, where it bridges actin filaments and plasma membrane proteins. Here, we demonstrate two specific morphogenetic roles of ezrin in the retinal pigment epithelium (RPE), i.e., the formation of very long apical microvilli and of elaborate basal infoldings typical of these cells, and characterize the role of ezrin in these processes using antisense and transfection approaches. In the adult rat RPE, only ezrin (no moesin or radixin) was detected at high levels by immunofluorescence and immunoelectron microscopy at microvilli and basal infoldings. At the time when these morphological differentiations develop, in the first two weeks after birth, ezrin levels increased fourfold to adult levels. Addition of ezrin antisense oligonucleotides to primary cultures of rat RPE drastically decreased both apical microvilli and basal infoldings. Transfection of ezrin cDNA into the RPE-J cell line, which has only trace amounts of ezrin and moesin, sparse and stubby apical microvilli, and no basal infoldings, induced maturation of microvilli and the formation of basal infoldings without changing moesin expression levels. Taken together, the results indicate that ezrin is a major determinant in the maturation of surface differentiations of RPE independently of other ERM family members. antisense retinal development cortical cytoskeleton epithelia ezrin radixin moesin proteins Footnotes Abbreviations used in this paper: ERM, ezrin/radixin/moesin family; HGF, hepatocyte growth factor; P, postnatal day; PR, photoreceptor; pAb, polyclonal antibody; RPE, retinal pigment epithelium; VSVG, vesicular stomatitis virus glycoprotein G. Submitted: 11 May 1999 Revision requested 17 November 1999 Accepted: 19 November 1999

Journal

The Journal of Cell Biology – Rockefeller University Press

Published: Dec 27, 1999

References

  • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane–cytoskeletal linker
    Algrain
  • Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrinin vivo imaging with GFP fusion proteins
    Amieva
  • Ezrin has properties to self-associate at the plasma membrane
    Andreoli
  • Membrane-actin microfilament connectionsan increasing diversity of players related to band 4.1
    Arpin
  • Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation
    Barila
  • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    Berryman
  • The retinal pigment epithelium, a versatile partner in vision
    Bok
  • Apical sorting of hemagluttinin by transcytosis in retinal pigment epithelium
    Bonilha
  • Development of the retinal pigment epithelium, choriocapillaris and Bruch's membrane in the albino rat
    Braekevelt
  • Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells
    Bretscher
  • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
    Bretscher
  • Regulation of cortical structure by the ezrin–radixin–moesin protein family
    Bretscher
  • Calcium phosphate-mediated gene transfera highly efficient transfection system for stably transforming cells with plasmid DNA
    Chen
  • The FERM domaina unique module involved in the linkage of cytoplasmic proteins to the membrane
    Chishti
  • Suppression of villin expression by antisense RNA impairs brush border assembly in polarized epithelial intestinal cells
    Costa de Beauregard
  • Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
    Crepaldi
  • A human retinal pigment epithelial cell line that retains epithelial characteristics after prolonged culture
    Davis
  • 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
  • Ezrin is a cyclic AMP-dependent protein kinase anchoring protein
    Dransfield
  • Relation of retinomotor responses and contractile proteins in vertebrate retinas
    Drenckhahn
  • Phagocytosis of rod outer segments by retinal pigment epithelial cells requires αvβ5 integrin for binding but not for internalization
    Finnemann
  • Villin induces microvilli growth and actin redistribution in transfected fibroblasts
    Friederich
  • Radixin is a novel member of the band 4.1 family
    Funayama
  • Janus kinases and focal adhesion kinases play in the 4.1 bandA superfamily of band 4.1 domains important for cell structure and signal transduction
    Girault
  • Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina
    Gundersen
  • The secretion-stimulated 80K phosphoprotein of parietal cells is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli
    Hanzel
  • Molecular motors, membrane movements and physiologyemerging roles for myosins
    Hasson
  • Molecular dissection of radixindistinct and interdependent functions of the amino- and carboxy-terminal domains
    Henry
  • Characterization of retinal pigment epithelial cells cultured on microporous filters
    Heth
  • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane associationpossible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    Hirao
  • Molecular heterogeneity of the actin filament cytoskeleton associated with microvilli of photoreceptors, muller glial cells and pigment epithelial cells of the retina
    Hofer
  • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    Kreis
  • Microtubules containing detyrosinated tubulin are less dynamic
    Kreis
  • Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts
    Lamb
  • Moesina member of the protein 4.1-talin–ezrin family of proteins
    Lankes
  • Myosin VIIa, the product of the Usher 1B syndrome gene, is concentrated in the connecting cilia of photoreceptor cells
    Liu
  • ERM proteins in cell adhesion and membrane dynamics
    Mangeat
  • Apical polarity of N-CAM and EMMPRIN in retinal pigment epithelium resulting from suppression of basolateral signal recognition
    Marmorstein
  • Ezrin NH2-terminal domain inhibits the cell extension activity of the COOH-terminal domain
    Martin
  • Three determinants in ezrin are responsible for cell extension activity
    Martin
  • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    Matsui
  • Immortalization of polarized rat retinal pigment epithelium
    Nabi
  • Increase in actin contents and elongation of apical projections in retinal pigmented epithelial cells during development of the chicken eye
    Owaribe
  • Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons
    Paglini
  • Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes
    Pestonjamasp
  • Protein kinase C-theta phosphorylation of moesin in the actin-binding sequence
    Pietromonaco
  • Identification of EBP50A PDZ-containing phosphoprotein that associates with members of the ezrin–radixin–moesin family
    Reczek
  • A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding
    Roy
  • Differential expression of the microspike-associated protein moesin in human tissues
    Schwartz-Albiez
  • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    Shaw
  • C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton
    Simons
  • Tissue culture of cat retinal pigment epithelium
    Stramm
  • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    Takahashi
  • Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members
    Takeuchi
  • A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junctionpurification and characterization
    Tsukita
  • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    Tsukita
  • A new 400-kD protein from isolated adherens junctionits localization at the undercoat of adherens junctions and at microfilament bundles such as stress fibers and circumferential bundles
    Tsukita
  • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    Turunen
  • The distribution of F-actin in cells isolated from vertebrate retinas
    Vaughan
  • Ezrin-calpain I interactions in gastric parietal cells
    Yao
  • Biochemical characterization of ezrin-actin interaction
    Yao
  • Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins
    Yonemura
  • Anatomy of the human retinal pigment epithelium
    Zinn