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| | [[8xd6]] – hRdx FERM domain 1-296 + MERS-CoV spike peptide – human<br /> |
| | [[8xd4]] – hRdx FERM domain + SARS-CoV spike peptide<br /> |
| [[1gc7]], [[2d2q]] – mRdx FERM domain – mouse <br /> | | [[1gc7]], [[2d2q]] – mRdx FERM domain – mouse <br /> |
| [[3x23]], [[2ems]], [[2yvc]], [[2d10]], [[2d11]], [[2emt]], [[1j19]], [[2zpy]] – mRdx FERM domain + peptide <br /> | | [[1j19]], [[2d10]], [[2d11]], [[2ems]], [[2emt]], [[2yvc]], [[2zpy]], [[3x23]] – mRdx FERM domain + peptide <br /> |
| [[1gc6]] – mRdx FERM domain + inositol-triphosphate<br /> | | [[1gc6]] – mRdx FERM domain + inositol-triphosphate<br /> |
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Latest revision as of 08:08, 17 September 2026
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Function
Radixin (Rdx) plays an important role in promoting cell migration by regulating Rac-1-mediated epithelial polarity and formation of adherens junctions through Rac guanine nucleotide exchange factors[1]. Rdx is part of the ERM (Ezrin/Radixin/Moesin) which is linked to cell shape change. Phosphorylation of the C-terminal Thr residues of ERM inhibits cell adhesion and induces formation of spherical cell shape[2].
Disease
Rdx deficiency causes increase in bilirubin in serum, a phenotype similar to that of Dubin-Johnson syndrome in human[3].
Structural highlights
The hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds[4]. Hydrophobic, Polar
- ↑ Valderrama F, Thevapala S, Ridley AJ. Radixin regulates cell migration and cell-cell adhesion through Rac1. J Cell Sci. 2012 Jul 15;125(Pt 14):3310-9. doi: 10.1242/jcs.094383. Epub 2012 Mar, 30. PMID:22467863 doi:https://dx.doi.org/10.1242/jcs.094383
- ↑ Tachibana K, Haghparast SM, Miyake J. Inhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin. Cell Adh Migr. 2015;9(6):502-12. doi: 10.1080/19336918.2015.1113366. PMID:26555866 doi:https://dx.doi.org/10.1080/19336918.2015.1113366
- ↑ Kikuchi S, Hata M, Fukumoto K, Yamane Y, Matsui T, Tamura A, Yonemura S, Yamagishi H, Keppler D, Tsukita S, Tsukita S. Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Nat Genet. 2002 Jul;31(3):320-5. doi: 10.1038/ng905. Epub 2002 Jun 17. PMID:12068294 doi:https://dx.doi.org/10.1038/ng905
- ↑ PMID: https://pubmed.ncbi.nlm.nih.gov/18706570/
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3D Structures of radixin
Updated on 17-September-2026
8xd6 – hRdx FERM domain 1-296 + MERS-CoV spike peptide – human
8xd4 – hRdx FERM domain + SARS-CoV spike peptide
1gc7, 2d2q – mRdx FERM domain – mouse
1j19, 2d10, 2d11, 2ems, 2emt, 2yvc, 2zpy, 3x23 – mRdx FERM domain + peptide
1gc6 – mRdx FERM domain + inositol-triphosphate
References
