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@ARTICLE{Zittlau:163264,
      author       = {Zittlau, Katharina I and Lechado-Terradas, Anna and Nalpas,
                      Nicolas and Geisler, Sven and Kahle, Philipp J and Macek,
                      Boris},
      title        = {{T}emporal {A}nalysis of {P}rotein {U}biquitylation and
                      {P}hosphorylation {D}uring {P}arkin-{D}ependent
                      {M}itophagy.},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {21},
      number       = {2},
      issn         = {1535-9476},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {DZNE-2022-00044},
      pages        = {100191},
      year         = {2022},
      note         = {(CC BY)},
      abstract     = {Mitophagy, the selective degradation of mitochondria by
                      autophagy, affects defective mitochondria following damage
                      or stress. At the onset of mitophagy, parkin ubiquitylates
                      proteins on the mitochondrial outer membrane. While the role
                      of parkin at the onset of mitophagy is well understood, less
                      is known about its activity during later stages in the
                      process. Here, we used HeLa cells expressing catalytically
                      active or inactive parkin to perform temporal analysis of
                      the proteome, ubiquitylome, and phosphoproteome during 18 h
                      after induction of mitophagy by mitochondrial uncoupler
                      carbonyl cyanide m-chlorophenyl hydrazine. Abundance
                      profiles of proteins downregulated in parkin-dependent
                      manner revealed a stepwise and 'outside-in' directed
                      degradation of mitochondrial subcompartments. While
                      ubiquitylation of mitochondrial outer membrane proteins was
                      enriched among early parkin-dependent targets, numerous
                      mitochondrial inner membrane, matrix, and cytosolic proteins
                      were also found ubiquitylated at later stages of mitophagy.
                      Phosphoproteome analysis revealed a possible crosstalk
                      between phosphorylation and ubiquitylation during mitophagy
                      on key parkin targets, such as voltage-dependent anion
                      channel 2.},
      keywords     = {HeLa Cells / Humans / Mitophagy / Phosphorylation /
                      Ubiquitin-Protein Ligases: metabolism / Ubiquitination /
                      mitochondria (Other) / mitophagy (Other) / parkin (Other) /
                      quantitative proteomics (Other) / ubiquitin (Other)},
      cin          = {AG Kahle 2},
      ddc          = {610},
      cid          = {I:(DE-2719)1210000-4},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34974192},
      pmc          = {pmc:PMC8808264},
      doi          = {10.1016/j.mcpro.2021.100191},
      url          = {https://pub.dzne.de/record/163264},
}