Suppression of the low-temperature phase-separated state under pressure in (Eu1−x_{1-x}Gdx_{x})0.6_{0.6}Sr0.4_{0.4}MnO3_{3} (x=0,0.1x=0,0.1)

We have demonstrated the effect of pressure on the steplike metamagnetic transition and its associated magnetostriction in (Eu$_{1-x}$Gd$_{x}$)$_{0.6}$Sr$_{0.4}$MnO$_{3}$ ($x=0$ and 0.1). The critical field initiating the field induced ferromagnetic transition in both samples is lowered by the applied pressure. The further application of external pressure up to 1.2 GPa on the $x=0$ parent sample causes a spontaneous ferromagnetic transition with a second-oder like character, leading to collapses of the steplike transition and its concomitant lattice striction. These findings indicate a crucial role of the low-temperature phase separated state characterized by a suppressed magnetization upon decreasing temperature.Comment: 8 pages, 6 figures. arXiv admin note: text overlap with arXiv:1006.145

Phosphorylation-dependent Akt-Inversin interaction at the basal body of primary cilia

A primary cilium is a microtubule-based sensory organelle that plays an important role in human development and disease. However, regulation of Akt in cilia and its role in ciliary development has not been demonstrated. Using yeast two-hybrid screening, we demonstrate that Inversin (INVS) interacts with Akt. Mutation in the INVS gene causes nephronophthisis type II (NPHP2), an autosomal recessive chronic tubulointerstitial nephropathy. Co-immunoprecipitation assays show that Akt interacts with INVS via the C-terminus. In vitro kinase assays demonstrate that Akt phosphorylates INVS at amino acids 864-866 that are required not only for Akt interaction, but also for INVS dimerization. Co-localization of INVS and phosphorylated form of Akt at the basal body is augmented by PDGF-AA. Akt-null MEF cells as well as siRNA-mediated inhibition of Akt attenuated ciliary growth, which was reversed by Akt reintroduction. Mutant phosphodeador NPHP2-related truncated INVS, which lack Akt phosphorylation sites, suppress cell growth and exhibit distorted lumen formation and misalignment of spindle axis during cell division. Further studies will be required for elucidating functional interactions of Akt-INVS at the primary cilia for identifying the molecular mechanisms underlying NPHP2