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@ARTICLE{LechadoTerradas:163312,
      author       = {Lechado Terradas, Anna and Zittlau, Katharina I and Macek,
                      Boris and Fraiberg, Milana and Elazar, Zvulun and Kahle,
                      Philipp J},
      title        = {{R}egulation of mitochondrial cargo-selective autophagy by
                      posttranslational modifications.},
      journal      = {The journal of biological chemistry},
      volume       = {297},
      number       = {5},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DZNE-2022-00092},
      pages        = {101339},
      year         = {2021},
      abstract     = {Mitochondria are important organelles in eukaryotes.
                      Turnover and quality control of mitochondria are regulated
                      at the transcriptional and posttranslational level by
                      several cellular mechanisms. Removal of defective
                      mitochondrial proteins is mediated by mitochondria resident
                      proteases or by proteasomal degradation of individual
                      proteins. Clearance of bulk mitochondria occurs via a
                      selective form of autophagy termed mitophagy. In yeast and
                      some developing metazoan cells (e.g., oocytes and
                      reticulocytes), mitochondria are largely removed by
                      ubiquitin-independent mechanisms. In such cases, the
                      regulation of mitophagy is mediated via phosphorylation of
                      mitochondria-anchored autophagy receptors. On the other
                      hand, ubiquitin-dependent recruitment of cytosolic autophagy
                      receptors occurs in situations of cellular stress or
                      disease, where dysfunctional mitochondria would cause
                      oxidative damage. In mammalian cells, a well-studied
                      ubiquitin-dependent mitophagy pathway induced by
                      mitochondrial depolarization is regulated by the
                      mitochondrial protein kinase PINK1, which upon activation
                      recruits the ubiquitin ligase parkin. Here, we review
                      mechanisms of mitophagy with an emphasis on
                      posttranslational modifications that regulate various
                      mitophagy pathways. We describe the autophagy components
                      involved with particular emphasis on posttranslational
                      modifications. We detail the phosphorylations mediated by
                      PINK1 and parkin-mediated ubiquitylations of mitochondrial
                      proteins that can be modulated by deubiquitylating enzymes.
                      We also discuss the role of accessory factors regulating
                      mitochondrial fission/fusion and the interplay with pro- and
                      antiapoptotic Bcl-2 family members. Comprehensive knowledge
                      of the processes of mitophagy is essential for the
                      understanding of vital mitochondrial turnover in health and
                      disease.},
      subtyp        = {Review Article},
      keywords     = {Animals / Mitochondria: genetics / Mitochondria: metabolism
                      / Mitochondrial Dynamics / Mitochondrial Proteins: genetics
                      / Mitochondrial Proteins: metabolism / Mitophagy / Signal
                      Transduction / Ubiquitination / autophagy (Other) /
                      mitochondria (Other) / phosphorylation (Other) / protein
                      kinase PINK1 (Other) / ubiquitin ligase parkin (Other) /
                      ubiquitylation (Other) / Mitochondrial Proteins (NLM
                      Chemicals)},
      cin          = {AG Kahle 2},
      ddc          = {540},
      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:34688664},
      pmc          = {pmc:PMC8591368},
      doi          = {10.1016/j.jbc.2021.101339},
      url          = {https://pub.dzne.de/record/163312},
}