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. 2017 Nov 2;7:14919. doi: 10.1038/s41598-017-15072-7

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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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Changes in the SlPIN1 phosphorylation levels and protein accumulation in the AZ during abscission. (a) SlPIN1 protein levels were detected by western blotting in the AZ at 0 h, 2 h, 4 h, 8 h, 16 h and 24 h after flower removal. Coomassie-staining Rubisco protein is shown for total loading control (lower panel, full image is shown in Supplementary Figure S2). (b) Amino acid sequence alignment of AtPIN1 (317–356) and SlPIN1 (312–345) in the region containing the phosphorylation sites (asterisk). The framed Ser are conserved in the SlPIN1 and AtPIN1. (c) The phosphorylation site Ser418 (asterisk) in the amino acid sequence of SlPIN1 (413–513) was mutagenized to Asp. (d) SlPIN1 phosphorylation site status in the AZ 0 h, 12 h and 24 h after flower removal following ethylene treatment.