Journal: PLOS ONE
Article Title: Ca 2+ -PP2B-PSD-95 axis: A novel regulatory mechanism of the phosphorylation state of Serine 295 of PSD-95
doi: 10.1371/journal.pone.0313441
Figure Lengend Snippet: (A) Western-blot analysis of the in-vitro dephosphorylation assay using mouse brain extracts. The “Control” sample (lane 1) was not subject to the dephosphorylation assay. (B) Quantification of dephosphorylation in vitro (pS295/PSD-95) incubated with calcium (Ca 2+ (+)) or without calcium (Ca 2+ (-)), relative to no-incubation (Control) conditions. The data are represented as the mean ± standard deviation (n = 3 from three independent experiments). *** P < 0.001 by the unpaired Student’s t -test; n.s., not significant. (C, D) Western-blot analysis (C) and quantification (D) of the efficiency of suppression by different doses of FK506 on the Ca 2+ -dependent dephosphorylation of pS295 in vitro . (E, F) Western-blot analysis (E) and quantification (F) showing that coapplication of FK506 and FKBP12 efficiently suppressed the Ca 2+ -dependent dephosphorylation of pS295 in vitro . The data are represented as the mean ± standard deviation overlaid with individual data points (n = 3 from three independent experiments). *** P < 0.001 by two-way ANOVA with the post-hoc Tukey’s multiple comparison test; n.s., not significant. F (1,16) = 383.3, P < 0.0001 for FKBP12+FK506, F (3,16) = 48.44, P < 0.0001 for Ca 2+ , and F (3,16) = 47.06, P < 0.0001 for interaction.
Article Snippet: NMDA was obtained from Sigma-Aldrich (St. Louis, MO, USA), EGTA from Wako Chemicals (Osaka, Japan), FK506 from ChemScene (Monmouth Junction, NJ, USA), ascomycin from Cayman Chemical (Ann Arbor, MI, USA), cyclosporine A from Nacalai Tesque (Kyoto, Japan), calyculin A from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and recombinant FKBP12 from R&D Systems (Minneapolis, MN, USA).
Techniques: Western Blot, In Vitro, De-Phosphorylation Assay, Control, Incubation, Standard Deviation, Comparison
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