Radixina
| Radixina | |
|---|---|
 | |
| Gene | |
| HUGO | RDX DFNB24 |
| Entrez | 5962 |
| Locus | Chr. 11 q22.3 |
| Proteina | |
| OMIM | 179410 |
| UniProt | P35241 |
La radixina è una proteina codificata negli esseri umani dal gene RDX[1][2][3].
È, insieme a ezrina e moesina, parte dalla famiglia delle proteine ERM, e funge da intermedio tra la membrana plasmatica e l'actina. Tramite ibridazione fluorescente in situ è stato localizzato il gene codificante a livello del cromosoma 11 (q23), sebbene ne siano state identificate due forme troncate codificate dagli pseudogeni RDXP2, localizzato a livello del cromosoma X (p21.3) e RDXP1, sempre a livello del cromosoma 11[3].
Note
- ↑ Wilgenbus KK, Milatovich A, Francke U, Furthmayr H, Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes, in Genomics, vol. 16, n. 1, giugno 1993, pp. 199–206, DOI:10.1006/geno.1993.1159, PMID 8486357.
- ↑ Khan SY, Ahmed ZM, Shabbir MI, Kitajiri S, Kalsoom S, Tasneem S, Shayiq S, Ramesh A, Srisailpathy S, Khan SN, Smith RJ, Riazuddin S, Friedman TB, Riazuddin S, Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24 locus, in Hum Mutat, vol. 28, n. 5, aprile 2007, pp. 417–23, DOI:10.1002/humu.20469, PMID 17226784.
- 1 2 Entrez Gene: RDX radixin, su ncbi.nlm.nih.gov.
Bibliografia
- Hoeflich KP, Ikura M, Radixin: cytoskeletal adopter and signaling protein, in Int. J. Biochem. Cell Biol., vol. 36, n. 11, 2005, pp. 2131–6, DOI:10.1016/j.biocel.2003.11.018, PMID 15313460.
- Matarrese P, Malorni W, Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death, in Cell Death Differ., 12 Suppl 1, 2006, pp. 932–41, DOI:10.1038/sj.cdd.4401582, PMID 15818415.
- Sato N, Funayama N, Nagafuchi A, et al., A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites, in J. Cell. Sci., vol. 103, n. 1, 1992, pp. 131–43, PMID 1429901.
- Hirao M, Sato N, Kondo T, et al., Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway, in J. Cell Biol., vol. 135, n. 1, 1996, pp. 37–51, DOI:10.1083/jcb.135.1.37, PMC 2121020, PMID 8858161.
- Bonaldo MF, Lennon G, Soares MB, Normalization and subtraction: two approaches to facilitate gene discovery, in Genome Res., vol. 6, n. 9, 1997, pp. 791–806, DOI:10.1101/gr.6.9.791, PMID 8889548.
- Stemmer-Rachamimov AO, Gonzalez-Agosti C, Xu L, et al., Expression of NF2-encoded merlin and related ERM family proteins in the human central nervous system, in J. Neuropathol. Exp. Neurol., vol. 56, n. 6, 1997, pp. 735–42, DOI:10.1097/00005072-199756060-00011, PMID 9184664.
- Takahashi K, Sasaki T, Mammoto A, et al., Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein, in J. Biol. Chem., vol. 272, n. 37, 1997, pp. 23371–5, DOI:10.1074/jbc.272.37.23371, PMID 9287351.
- Kondo T, Takeuchi K, Doi Y, et al., ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis, in J. Cell Biol., vol. 139, n. 3, 1997, pp. 749–58, DOI:10.1083/jcb.139.3.749, PMC 2141718, PMID 9348291.
- Murthy A, Gonzalez-Agosti C, Cordero E, et al., NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins, in J. Biol. Chem., vol. 273, n. 3, 1998, pp. 1273–6, DOI:10.1074/jbc.273.3.1273, PMID 9430655.
- Matsui T, Maeda M, Doi Y, et al., Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association, in J. Cell Biol., vol. 140, n. 3, 1998, pp. 647–57, DOI:10.1083/jcb.140.3.647, PMC 2140160, PMID 9456324.
- Yonemura S, Hirao M, Doi Y, et al., Ezrin/Radixin/Moesin (ERM) Proteins Bind to a Positively Charged Amino Acid Cluster in the Juxta-Membrane Cytoplasmic Domain of CD44, CD43, and ICAM-2, in J. Cell Biol., vol. 140, n. 4, 1998, pp. 885–95, DOI:10.1083/jcb.140.4.885, PMC 2141743, PMID 9472040.
- Bhartur SG, Goldenring JR, Mapping of ezrin dimerization using yeast two-hybrid screening, in Biochem. Biophys. Res. Commun., vol. 243, n. 3, 1998, pp. 874–7, DOI:10.1006/bbrc.1998.8196, PMID 9501018.
- Takahashi K, Sasaki T, Mammoto A, et al., Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl, in Oncogene, vol. 16, n. 25, 1998, pp. 3279–84, DOI:10.1038/sj.onc.1201874, PMID 9681826.
- Lamb RF, Roy C, Diefenbach TJ, et al., The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho, in Nat. Cell Biol., vol. 2, n. 5, 2000, pp. 281–7, DOI:10.1038/35010550, PMID 10806479.
- Vaiskunaite R, Adarichev V, Furthmayr H, et al., Conformational activation of radixin by G13 protein alpha subunit, in J. Biol. Chem., vol. 275, n. 34, 2000, pp. 26206–12, DOI:10.1074/jbc.M001863200, PMID 10816569.
- Hamada K, Shimizu T, Matsui T, et al., Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2, in Acta Crystallogr. D Biol. Crystallogr., vol. 57, Pt 6, 2001, pp. 891–2, DOI:10.1107/S0907444901005716, PMID 11375520.
- Kikuchi S, Hata M, Fukumoto K, et al., Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes, in Nat. Genet., vol. 31, n. 3, 2002, pp. 320–5, DOI:10.1038/ng905, PMID 12068294.
- Dickson TC, Mintz CD, Benson DL, Salton SR, Functional binding interaction identified between the axonal CAM L1 and members of the ERM family, in J. Cell Biol., vol. 157, n. 7, 2002, pp. 1105–12, DOI:10.1083/jcb.200111076, PMC 2173555, PMID 12070130.
- Haddad LA, Smith N, Bowser M, et al., The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton, in J. Biol. Chem., vol. 277, n. 46, 2003, pp. 44180–6, DOI:10.1074/jbc.M207211200, PMID 12226091.
Voci correlate
Altri progetti
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