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. 2015 Mar 30;6(17):15540–15550. doi: 10.18632/oncotarget.3702

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Copyright: © 2015 Ding et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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A. RAI16 interacted directly with PKA-RIIα. Flag-tagged RAI16 and Ha-tagged PKA-RIIα were co-expressed in HEK293TT cells. Left panel: Flag-tagged RAI16 was immunoprecipitated with anti-Flag antibody, and interacting proteins were verified with anti-Ha antibody; Right panel: Ha-tagged PKA-RIIα was immunoprecipitated with anti-Ha antibody and interacting Flag-tagged RAI16 were verified with anti-Flag antibody. B. Endogenous RAI16 in HEK293TT cells was immunoprecipitated with anti-RAI16 antibody and interacting endogenous PKA-RIIα were verified with anti-PKA-RIIα antibody. C. Flag-tagged RAI16 or its fragments or Aa352-370 deletion mutant (Δ352-370) was co-expressed with Ha-tagged PKA-RIIα. Cell lysates were used for immunoprecipitation to verify the interaction. D. An amphipathic helical wheel plot for amino acid residues Aa352-370 of RAI16 reveals a hydrophobic surface on one side (Orange). E. sHt31 and peptide 348-373 (sYF) could inhibit the interaction of RAI16 and PKA-RIIα. Flag-tagged RAI16 and Ha-tagged PKA-RIIα were co-expressed in HEK293TT cells. Cell lysates were used for immunoprecipitation to verify the interaction. F. Flag-tagged RAI16 was co-expressed with Ha-tagged PKA-RIIα full-length (FL), its D/D domain (Aa1-45), or its D/D domain deletion mutant (Δ1-45) in HEK293TT cells. Cell lysates were used for immunoprecipitation to verify the interaction. IB, immunoblot; IP, immunoprecipitation. G. Purified PKA-RIIα protein was coated on the microplate, and then was incubated with purified RAI16 protein alone or combinated with sHt31 or sYF, respectively. The interaction was detected by anti-RAI16 antibody and developed with HRP anti-rabbit IgG and TMB.