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. 2019 Oct 1;9:14128. doi: 10.1038/s41598-019-49912-5

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© The Author(s) 2019

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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Competitive PIRT binding between PIP₂ and TRPM8-S1S4. (a) NMR-detected titrations show hPIRT residues that bind both to PIP₂ and hTRPM8 (magenta) are generally localized to the intracellular amphipathic helix. Residues that exclusively bind PIP₂ (hTRPM8-S1S4) are colored red (blue). The overlapping binding regions indicate a competitive interaction for hPIRT. (b) Comparative binding affinities between PIP₂ and the hTRPM8-S1S4 domain to hPIRT show overlapping binding sites and a higher hPIRT affinity for hTRPM8-S1S4. (c) MST measurements highlight the apparent competitive binding relationship between hPIRT, hTRPM8-S1S4, and PIP₂ suggested by the NMR data. When hPIRT is titrated with the TRPM8-S1S4 domain in the presence of saturating PIP₂, the affinity curve shifts rightward, indicative of competition. MST K_d values are 5.3 ± 0.4, 36.5 ± 0.5, and 180 ± 60 millimole percent for hPIRT:hTRPM8-S1S4, hPIRT:hTRPM8-S1S4 + PIP₂, and hPIRT:PIP₂ respectively.