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Gene Review

Ezr  -  ezrin

Rattus norvegicus

Synonyms: Cytovillin, Ezrin, Vil2, Villin-2, p81
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Disease relevance of Vil2

  • METHODS: The expression of ezrin was examined in glomerular cells in culture, during kidney development, in the mature kidney, and in five different experimental kidney disease models in the rat [1].
  • Ezrin/moesin in motile Walker 256 carcinosarcoma cells: Signal-dependent relocalization and role in migration [2].

High impact information on Vil2


Biological context of Vil2

  • BACKGROUND: Ezrin belongs to a family of plasma membrane-cytoskeleton linking, actin binding proteins (Ezrin-radixin-Moesin family) involved in signal transduction, growth control, cell-cell adhesion, and microvilli formation [1].
  • Thus, estrogen stimulates the expression of ezrin and the LDLR in GH(3) cells, which interact physically and functionally to facilitate the endocytosis of LDL [5].
  • We propose that the up-regulation and interaction of ezrin and the LDLR serves to augment the delivery of cholesterol and other lipids in support of the hypertrophic and proliferative response of cells to estrogen [5].
  • The steady state levels of ezrin mRNA were found to increase in the fetal gut epithelium between day 15 and day 20 of gestation and during the first week after birth, in parallel with the morphogenetic process that leads to cell polarization and brush border assembly [6].
  • Inhibition of ezrin phosphorylation prevented its membrane association [2].

Anatomical context of Vil2

  • Addition of ezrin antisense oligonucleotides to primary cultures of rat RPE drastically decreased both apical microvilli and basal infoldings [4].
  • 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 [4].
  • Ezrin is specific for Schwann cells [7].
  • CONCLUSIONS: Ezrin likely has a role in the cytoskeletal organization, such as reassembling of acting filaments accompanying podocyte injury and regeneration [1].
  • The plasma membrane-actin linking protein, ezrin, is a glomerular epithelial cell marker in glomerulogenesis, in the adult kidney and in glomerular injury [1].

Associations of Vil2 with chemical compounds

  • Fractionation of cell lysates on sucrose density gradients shows ICAM-1 and ezrin to sediment at different densities, whereas ICAM-2 co-sediments with ezrin [8].
  • Two of these, annexin VII and annexin XI, were novel and had not been previously reported to be substrates of tyrosine kinases while the remaining two, ezrin and clathrin, have been reported to be tyrosine phosphorylated in some cell culture systems [9].
  • Partial purification of ERE-BP using three chromatography steps (Q-Sepharose, hydroxyapatite, and Sephacryl S300) followed by sodium dodecyl sulfate analysis indicated the presence of three major protein bands (p102, p81, and p48) as judged by Coomassie staining [10].
  • With the use of antibodies specific for NHERF and NHERF2, immunocytochemical analysis of rat kidney was undertaken to determine the nephron distribution of both proteins and their colocalization with other transporters and with ezrin [11].
  • Two of the DRI (differentially-expressed in rat intestine) genes are novel, while the others encode the microvillar protein ezrin and intracellular carrier proteins for retinol and fatty acids [12].

Regulatory relationships of Vil2


Other interactions of Vil2


Analytical, diagnostic and therapeutic context of Vil2


  1. The plasma membrane-actin linking protein, ezrin, is a glomerular epithelial cell marker in glomerulogenesis, in the adult kidney and in glomerular injury. Hugo, C., Nangaku, M., Shankland, S.J., Pichler, R., Gordon, K., Amieva, M.R., Couser, W.G., Furthmayr, H., Johnson, R.J. Kidney Int. (1998) [Pubmed]
  2. Ezrin/moesin in motile Walker 256 carcinosarcoma cells: Signal-dependent relocalization and role in migration. Rossy, J., Gutjahr, M.C., Blaser, N., Schlicht, D., Niggli, V. Exp. Cell Res. (2007) [Pubmed]
  3. Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton. Takeda, T., McQuistan, T., Orlando, R.A., Farquhar, M.G. J. Clin. Invest. (2001) [Pubmed]
  4. Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium. Bonilha, V.L., Finnemann, S.C., Rodriguez-Boulan, E. J. Cell Biol. (1999) [Pubmed]
  5. The low-density lipoprotein receptor is regulated by estrogen and forms a functional complex with the estrogen-regulated protein ezrin in pituitary GH3 somatolactotropes. Smith, P.M., Cowan, A., White, B.A. Endocrinology (2004) [Pubmed]
  6. Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation. Barilá, D., Murgia, C., Nobili, F., Perozzi, G. Biochim. Biophys. Acta (1995) [Pubmed]
  7. Nodes of Ranvier form in association with ezrin-radixin-moesin (ERM)-positive Schwann cell processes. Melendez-Vasquez, C.V., Rios, J.C., Zanazzi, G., Lambert, S., Bretscher, A., Salzer, J.L. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Ezrin and moesin co-localise with ICAM-1 in brain endothelial cells but are not directly associated. Romero, I.A., Amos, C.L., Greenwood, J., Adamson, P. Brain Res. Mol. Brain Res. (2002) [Pubmed]
  9. Annexin VII and annexin XI are tyrosine phosphorylated in peroxovanadate-treated dogs and in platelet-derived growth factor-treated rat vascular smooth muscle cells. Furge, L.L., Chen, K., Cohen, S. J. Biol. Chem. (1999) [Pubmed]
  10. Identification and characterization of an estrogen-responsive element binding protein repressed by estradiol. Gray, W.G., Gorski, J. Biochemistry (1996) [Pubmed]
  11. Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK. Wade, J.B., Welling, P.A., Donowitz, M., Shenolikar, S., Weinman, E.J. Am. J. Physiol., Cell Physiol. (2001) [Pubmed]
  12. Subtractive hybridization cloning of novel genes differentially expressed during intestinal development. Barilà, D., Murgia, C., Nobili, F., Gaetani, S., Perozzi, G. Eur. J. Biochem. (1994) [Pubmed]
  13. 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., Jay, D.G. Curr. Biol. (1997) [Pubmed]
  14. Peripheral astrocyte processes: monitoring by selective immunostaining for the actin-binding ERM proteins. Derouiche, A., Frotscher, M. Glia (2001) [Pubmed]
  15. Repeated electroconvulsive shock treatment increases the expression of A kinase anchoring proteins in the rat hippocampus. Lee, Y.I., Koo, Y.J., Cho, C.H., Seo, M., Kang, U.G., Kim, Y.S., Juhnn, Y.S. Neurosci. Lett. (2004) [Pubmed]
  16. Reciprocal regulation by estradiol 17-beta of ezrin and cadherin-catenin complexes in pituitary GH3 cells. Smith, P.M., Heinrich, C.A., Pappas, S., Peluso, J.J., Cowan, A., White, B.A. Endocrine (2002) [Pubmed]
  17. Proteomic identification of a large complement of rat urinary proteins. Thongboonkerd, V., Klein, J.B., Arthur, J.M. Nephron Exp. Nephrol. (2003) [Pubmed]
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