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. 2019 Sep 18;10:4251. doi: 10.1038/s41467-019-12203-8

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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 — Aggregation site III is a functional interaction site (aggregon) at the RGS domain surface. a Western blotting for GFP under native (upper panel) or denaturing conditions (lower panel) in lysates of U2OS cells transfected with indicated GFP-tagged constructs. b Western blotting under native (upper panel) or denaturing conditions (lower panel) for recombinant GST-RGS Cdt and GST-RGS Cdt QV-PS purified from bacteria. c Western blotting for GFP in lysates (L) of HEK293T cells transfected with GFP-Cdt 2–345 (Cdt 2–345) or the GFP-Cdt 2–345 QV-PS mutant (QV-PS 2–345) together with GFP, or in fractions of these lysates prepared via ultracentrifugation through a sucrose density gradient (fractions 2 [low density] to 20 [high density]). Distribution of GFP shows comparable fractionation of both samples. d Coomassie Brilliant Blue staining of proteins extracted from bacteria using SDS-containing (lanes 1–4) or Triton X-100-containing (lanes 5–8) lysis buffers, or purified by pulldown on glutathione beads (lane 9). Source data are provided as a Source Data file