Radixin

From Wikipedia, the free encyclopedia

Radixin

PDB rendering based on 1gc6.

Available structures: 1gc6, 1gc7, 1j19, 2d10, 2d11, 2d2q, 2yvc

Identifiers

Symbol(s)

RDX;

External IDs

OMIM: 179410 MGI: 97887 HomoloGene: 37707

Gene ontology
Molecular Function:	• actin binding • structural molecule activity
Cellular Component:	• cytoplasm • plasma membrane • microvillus • actin cytoskeleton
Biological Process:	• cytoskeletal anchoring • microvillus biogenesis • apical protein localization • barbed-end actin filament capping

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002906 (mRNA)
NP_002897 (protein)

NM_009041 (mRNA)
NP_033067 (protein)

Location

Chr 11: 109.61 - 109.67 Mb

Chr 9: 51.8 - 51.84 Mb

Pubmed search

[1]

[2]

Radixin, also known as RDX, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: RDX radixin.

[edit] 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, et al. (1992). "A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites.". J. Cell. Sci. 103 ( Pt 1): 131–43. PMID 1429901.
Wilgenbus KK, Milatovich A, Francke U, Furthmayr H (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.
Hirao M, Sato N, Kondo T, et al. (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. PMID 8858161.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Stemmer-Rachamimov AO, Gonzalez-Agosti C, Xu L, et al. (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. PMID 9184664.
Takahashi K, Sasaki T, Mammoto A, et al. (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. PMID 9287351.
Kondo T, Takeuchi K, Doi Y, et al. (1997). "ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis.". J. Cell Biol. 139 (3): 749–58. PMID 9348291.
Murthy A, Gonzalez-Agosti C, Cordero E, et al. (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. PMID 9430655.
Matsui T, Maeda M, Doi Y, et al. (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. PMID 9456324.
Yonemura S, Hirao M, Doi Y, et al. (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. 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, et al. (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.
Lamb RF, Roy C, Diefenbach TJ, et al. (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.
Vaiskunaite R, Adarichev V, Furthmayr H, et al. (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, et al. (2001). "Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2.". Acta Crystallogr. D Biol. Crystallogr. 57 (Pt 6): 891–2. PMID 11375520.
Kikuchi S, Hata M, Fukumoto K, et al. (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.
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. PMID 12070130.
Haddad LA, Smith N, Bowser M, et al. (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.