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. 2020 May 13;11:2399. doi: 10.1038/s41467-020-16118-7

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© The Author(s) 2020

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. 5 — a Mechanism of dopamine-sensitive AVATars: PACAP (blue) is modified with a tethered dopamine (DA) analog (black), and a DA-binding IgG (green) functions as the blocking domain. Free neurotransmitter (red) competes with this interaction, releasing active PACAP. Structure of thiol-reactive tethered DA shown at bottom. b Titration of PACAP-10,20-DA in the PAC1 cell assay, showing efficient receptor activation. c PAC1 receptor activation by 1 nM PACAP-10,20-DA in the absence (blue) or presence (green) of 600 nM DA-binding IgG. Activity is restored by addition of excess DA (red). Control IgG (gray) does not block PACAP activity. d Titration of the DA response of 1 nM DA-AVATar in the PAC1 activation assay. DA activates DA-AVATar with an EC₅₀ of 5.6 ± 0.5 µM. Error bars denote SD of duplicates.