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Figure 4. PERK auto-phosphorylation and kinase activity increases with the interaction of CN-A and PERK.(A) GST-cPERK and CN-Aα/B were incubated with [γ32P]ATP, resolved through 12% SDS-PAGE and visualized by autoradiography as described in Materials and Methods. Phosphorylation levels are shown for GST-cPERK in the presence (lanes 1 and 2) and absence (lanes 3 and 4) of CaM for high (H, 1.2 µM) and low (L, 30 nM) Ca2+, for GST-alone (lane 5), for GST-cPERK K/A in high Ca2+ (lane 6), for GST-cPERK without CN-A (lane 7) and for CN-A α/B without GST-cPERK (lane 8). Histogram corresponding to densitometric analysis of cPERK auto-phosphorylation (B) or CN-A phosphorylation (C) from the average of three independent experiments (n = 3), using as 100% control value lane 1 in B and lane 2 in C, respectively. See the Commassie blue gel for the loading control of the autoradiogram (Figure S6). (D) Kinase assay was performed as described above in the presence of 2 µM Ca2+, but adding increasing amounts of CN-Aα/B and in the presence of eIF2α (50 nM). Histogram corresponding to densitometric analysis of cPERK auto-phosphorylation (E) or CN-A phosphorylation (F) from three independent experiments (n = 3). One asterisk corresponds to a statistical significant difference (p<0.05, ANOVA test) and two asterisks denote a statistical significant difference of (p<0.001; ANOVA test). Image published in: Bollo M et al. (2010) Bollo et al. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution license Larger Image Printer Friendly View

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