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. 2018 Jan 26;50(1):e434. doi: 10.1038/emm.2017.247

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Copyright © 2018 The Author(s)

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/

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RpS3 is ubiquitinated by RNF138 in response to radiation. (a) Radiation-induced translocation of RNF138 from the cytoplasm to the nucleus was assessed by western blotting after cytoplasmic or nuclear fractionation. (b) RpS3–RNF138 interaction in U87MG and A172 cells after treatment with PI and irradiation was monitored by reciprocal IP assay. After preparation of NE, lysates were subjected to IP assay with an anti-rpS3 antibody or anti-RNF138 antibody followed by western blotting. (c) The effects of rpS3 WT or mut (ΔKH) on the interaction with RNF138 were measured by reciprocal IP assay. (d) The effects of RNF138 knockdown on the ubiquitination of rpS3 were measured. (e) The compensatory effects of RNF138 WT or mut (ΔRING or C18A/C54A) overexpression on the effects of RNF138 knockdown were determined.