PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy |
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| Authors: | Sumihiro Kawajiri Shinji Saiki Shigeto Sato Taku Hatano Nobutaka Hattori |
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| Institution: | a Department of Neurology, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan
b Research Institute for Disease of Old Age, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan |
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| Abstract: | Mutations in PTEN-induced putative kinase 1 (PINK1) cause recessive form of Parkinson’s disease (PD). PINK1 acts upstream of parkin, regulating mitochondrial integrity and functions. Here, we show that PINK1 in combination with parkin results in the perinuclear mitochondrial aggregation followed by their elimination. This elimination is reduced in cells expressing PINK1 mutants with wild-type parkin. Although wild-type PINK1 localizes in aggregated mitochondria, PINK1 mutants localization remains diffuse and mitochondrial elimination is not observed. This phenomenon is not observed in autophagy-deficient cells. These results suggest that mitophagy controlled by the PINK1/parkin pathway might be associated with PD pathogenesis.Structured summaryMINT-7557195: PINK1 (uniprotkb:Q9BXM7) physically interacts (MI:0915) with LC3 (uniprotkb:Q9GZQ8) by anti tag coimmunoprecipitation (MI:0007)MINT-7557109: LC3 (uniprotkb:Q9GZQ8) and PINK1 (uniprotkb:Q9BXM7) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-7557121: tom20 (uniprotkb:Q15388) and PINK1 (uniprotkb:Q9BXM7) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-7557138: parkin (uniprotkb:O60260), PINK1 (uniprotkb:Q9BXM7) and tom20 (uniprotkb:Q15388) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-7557173: LC3 (uniprotkb:Q9GZQ8) physically interacts (MI:0915) with PINK1 (uniprotkb:Q9BXM7) by anti bait coimmunoprecipitation (MI:0006) |
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| Keywords: | PTEN-induced putative kinase 1 Parkin Mitophagy Autophagy Parkinson&rsquo s disease |
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