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. 2018 Sep 6;14(12):2117–2138. doi: 10.1080/15548627.2018.1505153

Figure 8.

Figure 8.

p66SHC recruits LC3B-II and p-AMPK to depolarized mitochondria. (A,B) Immunoblot analysis of ubiquitin (left panel) or LC3B and p-AMPK (central and right panel) in lysates from purified mitochondria of the ctr and p66 MEC transfectants (A) or of the MEC transfectants expressing GFP-tagged wild-type p66SHC (p66GFP) or the GFP-tagged p66SHC LIR mutant (p66GFP-mLIR) (B), untreated or treated for 1 h with OA (n ≥ 3). PHB was used to assess the purity of mitochondrial fractions. The histograms in the lower part of central and right panel A-B show the quantification of LC3B and p-AMPK in multiple experiments (n ≥ 3). (C) Immunoblot analysis of GFP-specific immunoprecipitates from lysates of purified mitochondria from the MEC transfectants expressing GFP-tagged wild-type p66SHC (p66GFP) or the GFP-tagged p66SHC LIR mutant (p66GFP-mLIR) (n ≥ 3). Mitochondrial lysates were included in each gel to identify the migration of the proteins tested. (D) Immunoblot analysis of GFP-specific immunoprecipitates from lysates of purified mitochondria from the MEC transfectants expressing GFP-tagged wild-type p66SHC (p66GFP), untreated or treated for 3 h with OA, alone or in combination with epoxomicin (n = 3). The immunoblots shown are representative of 3 independent experiments. The data are expressed as mean± SD. **P ≤ 0.01; *P ≤ 0.05 (one-way ANOVA).