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. 2017 Sep 28;8:713. doi: 10.1038/s41467-017-00747-6

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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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Fig. 4 — MRAP2 interacts with and potentiates the activity of the GHS-R1a. a, b Co-immunoprecipitation of lysates from HEK293T cells transfected with 3HA-GHSR1a and MRAP2-3Flag. c Measurement of GHSR1a and MRAP2 interaction in live cells using the NanoBit assay. d Western blot detection of 3HA-GHSR1a and 3HA-GHSR1a-LgBit transfection in CHO cells. e Surface expression of GHSR1a in CHO cells transfected with 3HA-GHSR1a with or without MRAP2. f Total expression of GHSR1a in CHO cells transfected with 2HA-GHSR1a with or without MRAP2. g Ghrelin-induced IP3 production as measured by IP1 accumulation in CHO-M1 cells transfected with MRAP2, 3HA-GHSR1a alone (empty vector), or GHSR1a with human MRAP2. Error bars are SEM. ***p < 0.001