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. 2023 Jun 15;30(7):958–969. doi: 10.1038/s41594-023-01014-7

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© The Author(s) 2023

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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Extended Data Fig. 4 — (a) SEC-MALS analysis of F347A, W511A double mutant on the SNX1 (SNX1^†) interface that precludes its homodimerization. (b) Affinity pull down assay for mutants influencing SNX1 heterodimerization. (c) Tandem affinity purification of SNX5 induced homodimers. SNX5^WT was tagged with His-SUMO, and single (*) or triple (**) SNX5 mutants were tagged with GST. The complex was purified from combined cell lysates. Left lane shows the dimer with the His-SUMO tag still on SNX5. (d) Liposome tubulation ability of SNX1 and SNX5 proteins with mutations at interfaces affecting their dimerization capacity. Results in a-d are representative of two independent experiments.

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