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. 2017 Apr 5;12:666–673. doi: 10.1016/j.redox.2017.04.007

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© 2017 The Authors

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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Fig. 2. — Interaction between p53 and Parkin and p53 degradation in vitro and in vivo. (A) RAW264.7 cell lysates were immunoprecipitated with anti-p53 antibody and analyzed by immunoblotting with anti-Parkin antibody. (B) Molecular surface representation in the docking model of p53 with Parkin. (C) In vitro analysis of Parkin-mediated p53 ubiquitination. In vitro ubiquitination of p53 in the presence of Parkin. Reaction mixtures were analyzed by immunoblotting using the indicated antibodies. (D) In vivo ubiquitination assay in HEK293 cells transfected with plasmids expressing Flag-tagged p53, Myc-tagged Parkin, and HA-tagged ubiquitin. Cell lysates were immunoprecipitated with anti-p53 antibody and analyzed by immunoblotting with indicated antibodies. (E) In vivo ubiquitination assay of RAW 264.7 cells treated LPS (1 μg/ml). Cell lysates were immunoprecipitated with anti-ubiquitin antibody and analyzed by immunoblotting with indicated antibodies. (F) P53 expression in cytosolic and nuclear fractions. (G) P53 localization, as determined by immunofluorescence analysis and confocal microscope. Each band in the blots is representative of three experiments.