Radixin

From Proteopedia

spinqualitylabelsall models Mouse radixin FERM domain (grey) complex with N-terminal peptide of the adhesion molecule PSGL-1 (pink) (PDB code 2emt) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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 P-selectin glycoprotein ligand 1 with multiple hydrogen bonds[4].

3D Structures of radixin

Updated on 25-December-2017

1gc7, 2d2q – mRdx FERM domain – mouse
3x23, 2ems, 2yvc, 2d10, 2d11, 2emt, 1j19, 2zpy – mRdx FERM domain + peptide
1gc6 – mRdx FERM domain + inositol-triphosphate

References

1. ↑ 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:http://dx.doi.org/10.1242/jcs.094383
2. ↑ 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:http://dx.doi.org/10.1080/19336918.2015.1113366
3. ↑ 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:http://dx.doi.org/10.1038/ng905
4. ↑ . PMID:18706570