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. 2017 Sep 28;7:12389. doi: 10.1038/s41598-017-12585-z

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Effect of HRS on the degradation of CLR, CLRΔ9KR and RAMP2. (A,B) Cell lysates from experimental cells were analyzed by Western blotting and levels of HRS and β-actin quantified. (C,D) Cell-surface biotinylated HEK-CLR•RAMP2 and HEK-CLRΔ9KR•RAMP2 cells expressing HRS were not treated (NT) or challenged with AM (100 nM, 2-4 h), biotinylated proteins immunoprecipitated (IP) and Western blots (WB) probed for CLR (mouse-HA, mHA), CLRΔ9KR (mHA), RAMP2 (mouse-Myc, mMyc) and transferrin receptor (TfR, loading control). In untreated HEK-CLR•RAMP2 and HEK-CLRΔ9KR•RAMP2 cells, CLR, CLRΔ9KR, RAMP2 and TfR were readily detected. AM (100 nM, 4 h) induced degradation of CLR, CLRΔ9KR and RAMP2 to different levels. (E,F) Quantification of degradation of CLR, CLRΔ9KR and RAMP2. n = 4, Data were examined using ANOVA and Student-Newman-Keuls post-hoc test, *p < 0.05, **p < 0.01, ***p < 0.001.