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. 2016 Jul 26;7:12239. doi: 10.1038/ncomms12239

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(a) The mass spectra of the ICDI_1.4 peptide, showing phosphorylation at S1883. (b) Flow-cytometric FRET binding assays (c–e) between Venus-IQ-A_1.3 and Cerulean-ICDI_1.4 demonstrating the modulation of binding due to PKAc overexpression. (c) Overexpression of PKAc reduced binding between IQ-A_1.3 and wild-type ICDI_1.4. (d) Overexpression of PKAc did not affect binding between IQ-A_1.3 and ICDI_1.4 harboring an S1883A mutation. (e) Overexpression of PKAc reduced binding between IQ-A_1.3 and ICDI_1.4 harbouring an S1886A mutation. (f) Similar to wild-type Ca_V1.3_S/1.4DCT channels (Fig. 4c), Ca_V1.3_S/1.4DCT channels containing the S1883A mutation had minimal CDI. (g) Unlike wild-type Ca_V1.3_S/1.4DCT (Fig. 4d), Ca_V1.3_S/1.4DCT channels with the S1883A mutation did not exhibit increased CDI with overexpression of PKAc.