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Gene Review

EZR  -  ezrin

Gallus gallus

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High impact information on VIL2

  • The FERM (four point one, ezrin, radixin, and moesin) domain of talin engages integrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a prototype for FERM domain recognition of transmembrane receptors [1].
  • Several properties of this protein are identical to those of ezrin, a protein isolated from brush border and localized to motile elements of cultured cells [2].
  • In recent years, two proteins with a high degree of homology to ezrin were identified: moesin and radixin, together comprising the ERM protein family [3].
  • We previously identified a minor component of the marginal band by a monoclonal antibody, called 13H9 (Birgbauer and Solomon (1989). J. Cell Biol. 109, 1609-1620; Goslin et al. (1989). J. Cell Biol. 109, 1621-1631). mAb 13H9 also binds to the leading edges of fibroblasts and to neuronal growth cones and recognizes the cytoskeletal protein ezrin [3].
  • With the exception of calpactin I, the major tyrosine phosphoproteins detected in immunoblots appeared to be different from several previously characterized substrates of pp60v-src with similar molecular masses (ezrin, vinculin, and the fibronectin receptor) [4].

Biological context of VIL2

  • Since ezrin modulates cell morphology and cell adhesion profiles by linking membrane proteins with the cytoskeleton, it was suggested that ezrin is involved in the formation and/or maintenance of lamina-specific connections for neuronal subpopulations in the visual and somatosensory systems [5].

Anatomical context of VIL2


Other interactions of VIL2


Analytical, diagnostic and therapeutic context of VIL2

  • TB4 recognized a single 79-kDa protein on immunoblotting. cDNA cloning and immunochemical analysis revealed that the TB4 antigen molecule was ezrin, a cytoskeletal-membrane linker molecule belonging to the ezrin-radixin-moesin family [5].


  1. Structural determinants of integrin recognition by talin. García-Alvarez, B., de Pereda, J.M., Calderwood, D.A., Ulmer, T.S., Critchley, D., Campbell, I.D., Ginsberg, M.H., Liddington, R.C. Mol. Cell (2003) [Pubmed]
  2. A marginal band-associated protein has properties of both microtubule- and microfilament-associated proteins. Birgbauer, E., Solomon, F. J. Cell Biol. (1989) [Pubmed]
  3. Analysis of a cortical cytoskeletal structure: a role for ezrin-radixin-moesin (ERM proteins) in the marginal band of chicken erythrocytes. Winckler, B., González Agosti, C., Magendantz, M., Solomon, F. J. Cell. Sci. (1994) [Pubmed]
  4. Immunological characterization of proteins detected by phosphotyrosine antibodies in cells transformed by Rous sarcoma virus. Linder, M.E., Burr, J.G. J. Virol. (1988) [Pubmed]
  5. Specific expression of ezrin, a cytoskeletal-membrane linker protein, in a subset of chick retinotectal and sensory projections. Takahashi, M., Yamagata, M., Noda, M. Eur. J. Neurosci. (1999) [Pubmed]
  6. Restricted expression domains of Ezrin in developing epithelia of the chick. Richter, U., Wittler, L., Kessel, M. Gene Expr. Patterns (2004) [Pubmed]
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