Radixin

RDX
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1GC6, 1GC7, 1J19, 2D10, 2D11, 2D2Q, 2EMS, 2EMT, 2YVC, 2ZPY
Identifiers
Aliases	RDX, DFNB24, radixin
External IDs	OMIM: 179410; MGI: 97887; HomoloGene: 37707; GeneCards: RDX; OMA:RDX - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q22.3 Start 109,864,295 bp End 110,296,712 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 A5.3 Start 51,958,473 bp End 52,011,763 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex visceral pleura parietal pleura left adrenal gland left adrenal cortex ventricular zone corpus callosum secondary oocyte tibia Achilles tendon Top expressed in primary oocyte secondary oocyte Gonadal ridge cumulus cell zygote dermis atrium lacrimal gland abdominal wall pineal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein domain specific binding ATPase binding protein kinase A binding cytoskeletal protein binding protein binding actin binding RNA binding cadherin binding Cellular component cytoplasm membrane focal adhesion filopodium ruffle myelin sheath plasma membrane apical part of cell stereocilium microvillus apical plasma membrane cortical actin cytoskeleton cleavage furrow extracellular exosome cytoskeleton cell periphery lamellipodium midbody T-tubule cell tip extracellular space cell projection Biological process regulation of cell size establishment of endothelial barrier microvillus assembly regulation of organelle assembly establishment of protein localization positive regulation of cell migration regulation of GTPase activity positive regulation of G1/S transition of mitotic cell cycle negative regulation of homotypic cell-cell adhesion regulation of actin filament bundle assembly positive regulation of gene expression negative regulation of GTPase activity negative regulation of adherens junction organization apical protein localization actin filament capping cellular response to thyroid hormone stimulus regulation of cell shape protein kinase A signaling regulation of ruffle assembly positive regulation of protein localization to early endosome positive regulation of early endosome to late endosome transport negative regulation of cell size regulation of Rap protein signal transduction cellular response to platelet-derived growth factor stimulus barbed-end actin filament capping protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5962 19684 Ensembl ENSG00000137710 ENSMUSG00000032050 UniProt P35241 P26043 RefSeq (mRNA) NM_002906 NM_001260492 NM_001260493 NM_001260494 NM_001260495 NM_001260496 NM_001104616 NM_001104617 NM_009041 RefSeq (protein) NP_001247421 NP_001247422 NP_001247423 NP_001247424 NP_001247425 NP_002897 NP_001098086 NP_001098087 NP_033067 Location (UCSC) Chr 11: 109.86 – 110.3 Mb Chr 9: 51.96 – 52.01 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Radixin is a protein that in humans is encoded by the RDX gene.

Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses.

Interactions

Radixin has been shown to interact with GNA13.

See also

• ERM protein family

Further reading

• Hoeflich KP, Ikura M (2005). "Radixin: cytoskeletal adopter and signaling protein". Int. J. Biochem. Cell Biol. 36 (11): 2131–6. doi:10.1016/j.biocel.2003.11.018. PMID 15313460.
• Matarrese P, Malorni W (2006). "Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death". Cell Death Differ. 12 (Suppl 1): 932–41. doi:10.1038/sj.cdd.4401582. PMID 15818415.
• Sato N, Funayama N, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S (1992). "A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites". J. Cell Sci. 103 (1): 131–43. doi:10.1242/jcs.103.1.131. PMID 1429901.
• Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S (1996). "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway". J. Cell Biol. 135 (1): 37–51. doi:10.1083/jcb.135.1.37. PMC 2121020. PMID 8858161.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Stemmer-Rachamimov AO, Gonzalez-Agosti C, Xu L, Burwick JA, Beauchamp R, Pinney D, Louis DN, Ramesh V (1997). "Expression of NF2-encoded merlin and related ERM family proteins in the human central nervous system". J. Neuropathol. Exp. Neurol. 56 (6): 735–42. doi:10.1097/00005072-199756060-00011. PMID 9184664.
• Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai Y (1997). "Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein". J. Biol. Chem. 272 (37): 23371–5. doi:10.1074/jbc.272.37.23371. PMID 9287351.
• Kondo T, Takeuchi K, Doi Y, Yonemura S, Nagata S, Tsukita S (1997). "ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis". J. Cell Biol. 139 (3): 749–58. doi:10.1083/jcb.139.3.749. PMC 2141718. PMID 9348291.
• Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V (1998). "NHE-RF, a regulatory cofactor for Na( )-H exchange, is a common interactor for merlin and ERM (MERM) proteins". J. Biol. Chem. 273 (3): 1273–6. doi:10.1074/jbc.273.3.1273. PMID 9430655.
• Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S, Tsukita S (1998). "Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association". J. Cell Biol. 140 (3): 647–57. doi:10.1083/jcb.140.3.647. PMC 2140160. PMID 9456324.
• Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S (1998). "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". J. Cell Biol. 140 (4): 885–95. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
• Bhartur SG, Goldenring JR (1998). "Mapping of ezrin dimerization using yeast two-hybrid screening". Biochem. Biophys. Res. Commun. 243 (3): 874–7. doi:10.1006/bbrc.1998.8196. PMID 9501018.
• Takahashi K, Sasaki T, Mammoto A, Hotta I, Takaishi K, Imamura H, Nakano K, Kodama A, Takai Y (1998). "Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl". Oncogene. 16 (25): 3279–84. doi:10.1038/sj.onc.1201874. PMID 9681826. S2CID 21445282.
• Lamb RF, Roy C, Diefenbach TJ, Vinters HV, Johnson MW, Jay DG, Hall A (2000). "The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho". Nat. Cell Biol. 2 (5): 281–7. doi:10.1038/35010550. PMID 10806479. S2CID 25353057.
• Vaiskunaite R, Adarichev V, Furthmayr H, Kozasa T, Gudkov A, Voyno-Yasenetskaya TA (2000). "Conformational activation of radixin by G13 protein alpha subunit". J. Biol. Chem. 275 (34): 26206–12. doi:10.1074/jbc.M001863200. PMID 10816569.
• Hamada K, Shimizu T, Matsui T, Tsukita S, Tsukita S, Hakoshima T (2001). "Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2". Acta Crystallogr. D. 57 (Pt 6): 891–2. Bibcode:2001AcCrD..57..891H. doi:10.1107/S0907444901005716. PMID 11375520.
• Kikuchi S, Hata M, Fukumoto K, Yamane Y, Matsui T, Tamura A, Yonemura S, Yamagishi H, Keppler D, Tsukita S, Tsukita S (2002). "Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes". Nat. Genet. 31 (3): 320–5. doi:10.1038/ng905. PMID 12068294. S2CID 24961102.
• Dickson TC, Mintz CD, Benson DL, Salton SR (2002). "Functional binding interaction identified between the axonal CAM L1 and members of the ERM family". J. Cell Biol. 157 (7): 1105–12. doi:10.1083/jcb.200111076. PMC 2173555. PMID 12070130.
• Haddad LA, Smith N, Bowser M, Niida Y, Murthy V, Gonzalez-Agosti C, Ramesh V (2003). "The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton". J. Biol. Chem. 277 (46): 44180–6. doi:10.1074/jbc.M207211200. PMID 12226091.