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. 2018 Feb 23;8:3542. doi: 10.1038/s41598-018-21505-8

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© The Author(s) 2018

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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Substitution of serine for threonine at position 288 (S²⁸⁸) in ZnT2 leads to ZnT2 hyperphosphorylation. (a) Graphical representation of potential phosphorylation sites (serine, threonine and tyrosine) in wild-type ZnT2 (T²⁸⁸; left) and ZnT2 variant with a threonine to serine substitution (S²⁸⁸; right) as inferred from NetPhos 2.0. Green line represents potential phosphorylated serine residues; blue line represents potential phosphorylated threonine residues; pink line represents potential phosphorylated tyrosine residues; red horizontal line indicates threshold for modification potential; score indicates predicted phosphorylation potential score. (b) Representative immunoblot of phosphorylated serine in immunoprecipitates (IP) from MECs expressing T²⁸⁸ or S²⁸⁸. HA was used as normalization and input control. Cropped blots are displayed and full-length blots can be found in Supplementary Fig. S6a,b. (c) Quantification of serine phosphorylation. Data represent mean p-serine/HA ratio ± SD, n = 6 samples/genotype, from two independent experiments; p < 0.05*.