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. 2018 Aug 28;9:3491. doi: 10.1038/s41467-018-05924-9

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© The Author(s) 2018

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. 1 — TBC1d24 interacts with ephrinB2. a Co-immunoprecipitation assay (Co-IP) using gastrula embryos (stage 10) injected with TBC1d24-V5 RNA (500 pg) and ephrinB1-HA (300 pg), ephrinB2-HA (500 pg) or ephrinB3-HA RNAs (300 pg) show that TBC1d24 interacts with ephrinB2. b Illustration of serial deletion mutants from the C-terminus of ephrinB2. Co-IP using gastrula embryos injected with RNA encoding TBC1d24-V5 and HA-tagged ephrinB2 serial deletion mutants shows that the PDZ binding motif (Δ6) of ephrinB2 is required for TBC1d24 interaction. c Illustration of the amino acid stretches representing regions deleted within the TBC domain. Co-IP using gastrulas injected with RNA for ephrinB2-HA and TBC1d24-V5 serial deletion mutants shows that the F region within the TBC domain of TBC1d24 is critical for an ephrinB2 interaction. d Immunofluorescence microscopic analysis (IF) shows that membrane localisation of V5-tagged TBC1d24 was induced by wild-type ephrinB2 but not ephrinB2-Δ4. Animal caps were dissected at stage 10 and then immunostained for ephrinB2 (red) and TBC1d24 (green). Bar, 50 μm