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. 2017 Sep 12;7:11328. doi: 10.1038/s41598-017-11102-6

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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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Type-1 myosins interact with Htt25QP. (a) Schematic picture showing protein domains of endocytic factors important for detoxifying Htt25QP containing either proline-rich regions themselves, and/or proline-rich region-binding domains. (MYO3 did not show genetic interactions with HTT25QP, but is shown due to its redundancy with MYO5 and data presented below.) Illustrations are made using Pfam and Prosite. The proline-rich sequences are manually created. (b) and (c) In vitro binding assay between immobilized GFP proteins on GFP-Trap agarose beads and indicated SH3 domain-containing proteins. Blots are stained with PonceauS for visualization of total proteins and probed for TAP-tagged proteins using an anti-CBP antibody and GFP tagged proteins using an anti-GFP antibody. Representative pictures from two (Sla1, Bzz1, and Rvs167) or three (Myo5 and Myo3) independent experiments are shown (the binding of Myo5 to Htt103QP was analyzed two times). (Full-length blots are shown in Fig. S12).