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. 2019 Mar 19;10:1261. doi: 10.1038/s41467-019-09204-y

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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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Fig. 3 — Conformational change of arrestins depend on phosphorylation pattern. a Limited trypsin digest of arrestin-1, -2 and -3 in presence of non- (0P) and fully phosphorylated (7P) phosphopeptide analogs of the rhodopsin C-terminus. The presence of fully phosphorylated peptide resulted in a change of the digestion pattern from three to two bands in comparison to nonphosphorylated peptide for arrestin-1 and -3. The digestion of arrestin-2 always resulted in two bands with similar molecular weight as arrestin-1/-3 independent of which peptide was present. However, digestion was accelerated in the presence of fully phosphorylated peptide as compared to nonphosphorylated peptide. b Limited trypsin digestion of arrestin-1 in the presence of different tri-phosphorylated peptides. Peptide-induced conformational changes in arrestin-1 are indicated by a change in the digest pattern (green boxes) (Source data are provided as a Source Data file.)