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. 2017 Nov 15;7:15623. doi: 10.1038/s41598-017-15855-y

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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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TRPM6 mediates divalent-cation influx. (a) Zinc-influx assay was employed to assess the channel function of XTRPM6, hTRPM6, mTRPM7, and XTRPM7 in intact cells. hTRPM6 and mTRPM7 were used as positive controls. Uptake of Zn²⁺ could be detected in TRPM7^−/− HEK293T cells transiently transfected with XTRPM6, XTRPM7, mTRPM7, and hTRPM6. Zn²⁺-uptake by XTRPM6, hTRPM6, and XTRPM7 could be pharmacologically enhanced by application of 250 μM 2-APB, whereas Zn²⁺-uptake by mTRPM7 was suppressed by application of 250 μM 2-APB. (b and c) Quantification of fluorescence intensity expressed in arbitrary units (a.u.) from the results shown in (a).