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
Gene location (Human)
Chr.	Chromosome 11 (human)
End	110,296,712 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	52,011,763 bp
RNA expression pattern
	Top expressed in
	visceral pleura; ; parietal pleura; ; left adrenal gland; ; corpus callosum; ; secondary oocyte; ; tibia; ; Achilles tendon; ; biceps brachii; ; ganglionic eminence; ; metanephric glomerulus;
	Top expressed in
	secondary oocyte; ; cumulus cell; ; dermis; ; atrium; ; lacrimal gland; ; abdominal wall; ; pineal gland; ; seminal vesicula; ; left lung lobe; ; otic placode;
	More reference expression data
	; ; ; ;
	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
	5962
	19684
	ENSG00000137710
	ENSMUSG00000032050
	P35241
	P26043
NM_002906; NM_001260492; NM_001260493; NM_001260494; NM_001260495;
	NM_001260496
	NM_001104616; NM_001104617; NM_009041
NP_001247421; NP_001247422; NP_001247423; NP_001247424; NP_001247425;
	NP_002897
	NP_001098086; NP_001098087; NP_033067
	Wikidata
View/Edit Human	View/Edit Mouse

Radixin is a protein that in humans is encoded by the RDX gene.^[5]^[6]^[7]

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.^[7]

Interactions

Radixin has been shown to interact with GNA13.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000137710 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032050 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Wilgenbus KK, Milatovich A, Francke U, Furthmayr H (June 1993). "Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes". Genomics. 16 (1): 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 (April 2007). "Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24 locus". Hum Mutat. 28 (5): 417–23. doi:10.1002/humu.20469. PMID 17226784. S2CID 7671031.
1 2 "Entrez Gene: RDX radixin".
↑ Vaiskunaite R, Adarichev V, Furthmayr H, Kozasa T, Gudkov A, Voyno-Yasenetskaya TA (August 2000). "Conformational activation of radixin by G13 protein alpha subunit". J. Biol. Chem. 275 (34): 26206–12. doi:10.1074/jbc.M001863200. PMID 10816569.

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000137710 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032050 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8486357-5] Wilgenbus KK, Milatovich A, Francke U, Furthmayr H (June 1993). "Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes". Genomics. 16 (1): 199–206. doi:10.1006/geno.1993.1159. PMID 8486357.

[pmid17226784-6] 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 (April 2007). "Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24 locus". Hum Mutat. 28 (5): 417–23. doi:10.1002/humu.20469. PMID 17226784. S2CID 7671031.

[entrez-7] 1 2 "Entrez Gene: RDX radixin".

[pmid10816569-8] Vaiskunaite R, Adarichev V, Furthmayr H, Kozasa T, Gudkov A, Voyno-Yasenetskaya TA (August 2000). "Conformational activation of radixin by G13 protein alpha subunit". J. Biol. Chem. 275 (34): 26206–12. doi:10.1074/jbc.M001863200. PMID 10816569.

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Interactions

See also

References

Further reading