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. 2017 Dec 8;7:17233. doi: 10.1038/s41598-017-17371-5

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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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HuR regulates GM-CSF mRNA by binding and stabilizing its 3′UTR in Th17 cells. (a) Schematic diagram of RIP analysis. (b) RIP analysis was performed to detect GM-CSF mRNA enrichment after IP using anti-HuR (3A2) or isotype–matched antibody (IgG1) from Th17 cell cytoplasmic extracts. IL-23R mRNA was assayed as a negative control. (c–e) Biotin pulldown was used to determine whether HuR directly binds to 3′UTR of GM-CSF mRNA. (c,d) Schematic diagrams of biotin probe corresponding to GM-CSF and 3′UTR and biotin-pull down assay, respectively. (e) HuR protein could be detected by Western blot in biotinylated transcripts spanning GM-CSF 3′UTR, but not in GM-CSF mRNA ORF biotinylated transcripts. GAPDH biotinylated transcripts were unreactive (e). One of two independent experiments is shown in (e). **p < 0.01.