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. 2018 May 16;8:7682. doi: 10.1038/s41598-018-25815-9

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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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Identification of a protein that interacts with NiV V. (A) Myc-tagged NiV V and a mutant lacking the C-terminal domain (ΔCT) were expressed in HEK293T cells. At 48 h posttransfection, an immunoprecipitation assay was performed, and the precipitated proteins were detected with silver staining. The band indicated by the arrowhead was analyzed with mass spectrometry. *Nontargeted bands. (B) The immunoprecipitation assay was performed as described in (A), and the precipitated proteins were detected with western blotting. (C) Myc-tagged NiV V was expressed in HEK293T cells, and at 48 h posttransfection, an immunoprecipitation assay was performed using UBXN1-specific antibody. The precipitated proteins were detected with western blotting. (D) Myc-tagged NiV V expressed in HeLa cells was immunoprecipitated, and the precipitated proteins were detected with western blotting. (E) Myc-tagged NiV V or ΔCT were expressed together with HA-tagged UBXN1 in HEK293T cells, and after 48 h, an immunoprecipitation assay was performed with anti-myc or anti-HA antibody. The precipitated proteins were detected with western blotting. (F) NiV V and HA-tagged UBXN1 were expressed in HEK293T cells, and after 24 h, an indirect immunofluorescence assay was performed. The subcellular localization of NiV V and UBXN1 was observed with confocal microscopy. (G) NiV V was expressed in HeLa cells, and the subcellular localization of NiV V and endogenous UBXN1 was examined by an indirect immunofluorescence assay. The gel and blots presented in (A–E) were cropped from different images to improve clarity. Full-length gel and blots are presented in Supplementary Figure S1.