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. 2021 Apr 16;53(4):667–680. doi: 10.1038/s12276-021-00596-w

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© The Author(s) 2021

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. 5 — a Immunoblot analysis of whole-cell lysates and CoIP assays using HEK293T cells. Flag immunoprecipitates were isolated from HEK293T cells transfected with His-OPTN or Flag-Nrf2 plasmids for 1 d. The IP bands showed that Flag-tagged NRF2 can pull down His-tagged OPTN, indicating that NRF2 and OPTN can bind with each other in vitro. β-Actin expression served as a loading control. b Intracellular localization of OPTN and NRF2 in preosteoclasts. The Optn^−/− and Optn^+/+ preosteoclasts were treated with M-CSF (10 ng/mL) and RANKL (30 ng/mL) for 6, 12, 24, and 72 h. RANKL + 5 μM curcumin treatment for 72 h was used as a positive control. After fixation, the cells were processed with immunofluorescence using antibodies against OPTN (green), NRF2 (red) and nuclei (blue). In merged images, colocalization of OPTN and NRF2 was observed mostly in perinuclear granular structures (yellow). Scale bar = 10 μm.