The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RDX  -  radixin

Gallus gallus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on RDX

  • We have assayed the domains of the ERM protein radixin for binding activities in vitro [1].
  • Affinity columns bearing the amino-terminal domain of radixin selectively bound a small subset of the proteins of the chicken erythrocyte cytoskeleton [1].
  • Both ezrin and radixin localize to the position of the marginal band [2].
  • Withdrawal of nerve growth factor (NGF) induces rapid collapse of the growth cones; concomitantly, radixin staining in these growth cones are greatly diminished [3].
  • These results suggest that CLIC5 associates with radixin in hair cell stereocilia and may help form or stabilize connections between the plasma membrane and the filamentous actin core [4].

Biological context of RDX


Anatomical context of RDX

  • The results demonstrate that radixin is the major ERM protein associated with the cytoskeleton [2].
  • We show that the radixin staining of the growth cones is also asymmetrically localized toward the leading edges in the new direction of growth [3].
  • The ERM protein--ezrin, radixin, moesin--localize to a variety of cortical structures, where they may participate in connecting the cytoskeleton to components of the plasma membrane [3].
  • Refined immunolocalization in rat and chicken vestibular hair cells showed that CLIC5 is limited to the basal region of the hair bundle, similar to the known location of radixin [4].
  • By mass spectrometry and immunoblotting, CLIC5 was shown to be expressed at high levels in stereocilia of the chicken utricle, in an approximate 1:1 molar ratio with radixin [4].


  1. Interdomain interactions of radixin in vitro. Magendantz, M., Henry, M.D., Lander, A., Solomon, F. J. Biol. Chem. (1995) [Pubmed]
  2. 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]
  3. Response of radixin to perturbations of growth cone morphology and motility in chick sympathetic neurons in vitro. Gonzalez-Agosti, C., Solomon, F. Cell Motil. Cytoskeleton (1996) [Pubmed]
  4. The chloride intracellular channel protein CLIC5 is expressed at high levels in hair cell stereocilia and is essential for normal inner ear function. Gagnon, L.H., Longo-Guess, C.M., Berryman, M., Shin, J.B., Saylor, K.W., Yu, H., Gillespie, P.G., Johnson, K.R. J. Neurosci. (2006) [Pubmed]
  5. Cloning and expression profile of chicken radixin. Li, W., Crouch, D.H. Biochim. Biophys. Acta (2000) [Pubmed]
WikiGenes - Universities