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)
 

Links

 

Gene Review

Rdx  -  radixin

Mus musculus

Synonyms: AA516625, ESP10, Radixin
 
 
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

  • Here we show that Rdx(-/-) mice are normal at birth, but their serum concentrations of conjugated bilirubin begin to increase gradually around 4 weeks, and they show mild liver injury after 8 weeks [1].
  • Radixin (encoded by Rdx) is the dominant ERM protein in the liver of wildtype mice and is concentrated at bile canalicular membranes (BCMs) [1].
  • Ezrin protein levels in Vil2(kd/kd) stomachs decreased to <5% of the wild-type levels without compensatory up-regulation of radixin or moesin [2].
  • In Rdx(-)(/)(-) mice, ezrin appeared to compensate for radixin deficiency in terms of the development of cochlear stereocilia and the development/maintenance of vestibular stereocilia [3].
  • We found that in cochlear and vestibular sensory hair cells of adult wild-type mice, radixin was specifically enriched in stereocilia, specially developed giant microvilli, and that radixin-deficient (Rdx(-)(/)(-)) adult mice exhibited deafness but no obvious vestibular dysfunction [3].
 

Biological context of Rdx

  • Activated mutant that mimics the phosphorylated state of radixin (T564E) stimulated Rac1, induced the phosphorylation of CaMKII, and stimulated SRE-dependent gene transcription [4].
  • We determined the effects of the N-terminal domain (amino acids 1-318) and C-terminal domain (amino acids 319-583) of radixin on serum response element (SRE)-dependent gene transcription initiated by a constitutively activated Galpha(13)Q226L [4].
  • Down-regulation of endogenous radixin using small interference RNA inhibited SRE-dependent gene transcription and phosphorylation of CaMKII induced by Galpha(13)Q226L [4].
  • Low level expression of full-length radixin or either of the truncated polypeptides has no detectable effect on cell physiology [5].
  • These exons encode a FERM (F, ezrin, radixin and moesin) domain that may interact with integral membrane proteins [6].
 

Anatomical context of Rdx

 

Associations of Rdx with chemical compounds

  • Lysophosphatidic acid treatment led to phosphorylation of radixin preceding its redistribution into apical protrusions [10].
  • The encoded protein, Merlin, is closely related to the Ezrin, Radixin, and Moesin family of membrane/cytoskeletal linker proteins [11].
  • Significantly, cotransfection of RhoAV14 or C3 transferase with radixin and moesin revealed that RhoA activity is necessary and sufficient for their phosphorylation [10].
  • It has been previously shown that the active form of radixin can bind in vitro to Dbl, a Rho-specific guanine nucleotide exchange factor, although an in vivo interaction has not yet been demonstrated [12].
  • Moreover, we also found that radixin mRNA and its protein levels are under DA control through specific D1-dopaminergic receptors in a dose- and time-dependent manner in the GT1-7 neural cell line [13].
 

Other interactions of Rdx

  • Overall, our results indicated that radixin via its C-terminal domain mediates SRE-dependent gene transcription through activation of Rac1 and CaMKII [4].
  • When co-transfected with Galpha(13)Q226L, the C-terminal domain of radixin synergistically stimulated the SRE activation; RhoGDI inhibited this effect [4].
  • Results obtained from yeast two-hybrid screening, blot overlay binding assays, and coimmunoprecipitations demonstrate that BPAG1n4 interacts directly with dynactin p150Glued through its unique ezrin/radixin/moesin domain [14].
  • We show that lysophosphatidic acid stimulation of serum-starved NIH3T3 cells resulted in relocalization of radixin into apical membrane/actin protrusions, which was blocked by inactivation of Rho by C3 transferase [10].
 

Analytical, diagnostic and therapeutic context of Rdx

References

  1. Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Kikuchi, S., Hata, M., Fukumoto, K., Yamane, Y., Matsui, T., Tamura, A., Yonemura, S., Yamagishi, H., Keppler, D., Tsukita, S., Tsukita, S. Nat. Genet. (2002) [Pubmed]
  2. Achlorhydria by ezrin knockdown: defects in the formation/expansion of apical canaliculi in gastric parietal cells. Tamura, A., Kikuchi, S., Hata, M., Katsuno, T., Matsui, T., Hayashi, H., Suzuki, Y., Noda, T., Tsukita, S., Tsukita, S. J. Cell Biol. (2005) [Pubmed]
  3. Radixin deficiency causes deafness associated with progressive degeneration of cochlear stereocilia. Kitajiri, S., Fukumoto, K., Hata, M., Sasaki, H., Katsuno, T., Nakagawa, T., Ito, J., Tsukita, S., Tsukita, S. J. Cell Biol. (2004) [Pubmed]
  4. Radixin stimulates Rac1 and Ca2+/calmodulin-dependent kinase, CaMKII: cross-talk with Galpha13 signaling. Liu, G., Voyno-Yasenetskaya, T.A. J. Biol. Chem. (2005) [Pubmed]
  5. Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains. Henry, M.D., Gonzalez Agosti, C., Solomon, F. J. Cell Biol. (1995) [Pubmed]
  6. The motor and tail regions of myosin XV are critical for normal structure and function of auditory and vestibular hair cells. Anderson, D.W., Probst, F.J., Belyantseva, I.A., Fridell, R.A., Beyer, L., Martin, D.M., Wu, D., Kachar, B., Friedman, T.B., Raphael, Y., Camper, S.A. Hum. Mol. Genet. (2000) [Pubmed]
  7. Differential expression of ezrin/radixin/moesin (ERM) and ERM-associated adhesion molecules in the blastocyst and uterus suggests their functions during implantation. Matsumoto, H., Daikoku, T., Wang, H., Sato, E., Dey, S.K. Biol. Reprod. (2004) [Pubmed]
  8. Radixin is a novel member of the band 4.1 family. Funayama, N., Nagafuchi, A., Sato, N., Tsukita, S., Tsukita, S. J. Cell Biol. (1991) [Pubmed]
  9. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A., Tsukita, S. J. Cell Biol. (1994) [Pubmed]
  10. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Shaw, R.J., Henry, M., Solomon, F., Jacks, T. Mol. Biol. Cell (1998) [Pubmed]
  11. Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli. Shaw, R.J., McClatchey, A.I., Jacks, T. J. Biol. Chem. (1998) [Pubmed]
  12. Phosphorylation-independent membrane relocalization of ezrin following association with Dbl in vivo. Vanni, C., Parodi, A., Mancini, P., Visco, V., Ottaviano, C., Torrisi, M.R., Eva, A. Oncogene (2004) [Pubmed]
  13. Changes in cytoskeletal gene expression linked to MPTP-treatment in Mice. Cuadrado-Tejedor, M., Sesma, M.T., Giménez-Amaya, J.M., Ortiz, L. Neurobiol. Dis. (2005) [Pubmed]
  14. BPAG1n4 is essential for retrograde axonal transport in sensory neurons. Liu, J.J., Ding, J., Kowal, A.S., Nardine, T., Allen, E., Delcroix, J.D., Wu, C., Mobley, W., Fuchs, E., Yang, Y. J. Cell Biol. (2003) [Pubmed]
  15. 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]
 
WikiGenes - Universities