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. 2021 Jan 4;22(1):e50854. doi: 10.15252/embr.202050854

Figure 1. MOAP‐1 localizes at the p62 bodies upon exposure to cellular stresses.

Figure 1

  1. MOAP‐1 colocalizes with p62 in the cytoplasmic inclusion bodies upon proteasome inhibition. HCT116 cells were transfected with plasmid encoding GFP‐MOAP‐1 or GFP only control. 14 h later, cells were treated with the proteasome inhibitor MG132 (5 µM) for 8 h and analyzed by immunofluorescence (IF) with anti‐GFP (in green) and anti‐p62 (in red) antibodies. Scale bar: 5 µm.
  2. Endogenous MOAP‐1 resides at the p62 bodies upon proteasome inhibition. HCT116 cells were treated with MG132 (5 µM) for 8 h and analyzed by IF with anti‐MOAP‐1 (in green) and anti‐p62 (in red) antibodies. Scale bar: 5 µm.
  3. MOAP‐1 is recruited to the p62 bodies upon exposure to cellular stresses. LO2 hepatocytes were transfected with plasmid encoding Myc‐MOAP‐1. 14 h later, cells were then treated with MG132 (5 µM), arsenic trioxide (As2O3, 10 µM) or diethylnitrosamine (DEN, 200 µM) for 8 h each. Cells were then processed for IF analysis with anti‐Myc (in green) and anti‐p62 (in red) antibodies. Scale bar: 5 µm.
  4. MOAP‐1 spontaneously localizes to the p62 bodies at resting state in the liver cancer cell lines, HepG2, Huh‐1, JHH5 and JHH7. The liver cancer cell lines were transfected with the plasmid encoding Myc‐MOAP‐1. 14 h later, transfected cells were subjected to IF analysis with anti‐Myc (in green) and anti‐p62 (in red) antibodies. Scale bar: 5 µm.
  5. Absence of the aggregated patterns of MOAP‐1 in the p62 deficient cells. WT and p62 KO HepG2 cells were transfected with plasmid encoding Myc‐MOAP‐1 for 14 h and the cells were subjected to IF analysis as in (D). Scale bar: 5 µm.
  6. Western blotting analysis of p62 and Myc‐MOAP‐1 protein levels in the WT and p62 KO HepG2 cells as described in (E). Actin as loading control.

Data information: In (A–E), nuclei were counterstained with DAPI (blue).

Source data are available online for this figure.