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@ARTICLE{Runkel:141390,
      author       = {Runkel, Eva D and Liu, Shu and Baumeister, Ralf and
                      Schulze, Ekkehard},
      title        = {{S}urveillance-activated defenses block the {ROS}-induced
                      mitochondrial unfolded protein response.},
      journal      = {PLoS Genetics},
      volume       = {9},
      number       = {3},
      issn         = {1553-7404},
      address      = {San Francisco, Calif.},
      publisher    = {Public Library of Science},
      reportid     = {DZNE-2020-07712},
      pages        = {e1003346},
      year         = {2013},
      abstract     = {Disturbance of cellular functions results in the activation
                      of stress-signaling pathways that aim at restoring
                      homeostasis. We performed a genome-wide screen to identify
                      components of the signal transduction of the mitochondrial
                      unfolded protein response (UPR(mt)) to a nuclear chaperone
                      promoter. We used the ROS generating complex I inhibitor
                      paraquat to induce the UPR(mt), and we employed RNAi
                      exposure post-embryonically to allow testing genes whose
                      knockdown results in embryonic lethality. We identified 54
                      novel regulators of the ROS-induced UPR(mt). Activation of
                      the UPR(mt), but not of other stress-signaling pathways,
                      failed when homeostasis of basic cellular mechanisms such as
                      translation and protein transport were impaired. These
                      mechanisms are monitored by a recently discovered
                      surveillance system that interprets interruption of these
                      processes as pathogen attack and depends on signaling
                      through the JNK-like MAP-kinase KGB-1. Mutation of kgb-1
                      abrogated the inhibition of ROS-induced UPR(mt), suggesting
                      that surveillance-activated defenses specifically inhibit
                      the UPR(mt) but do not compromise activation of the heat
                      shock response, the UPR of the endoplasmic reticulum, or the
                      SKN-1/Nrf2 mediated response to cytosolic stress. In
                      addition, we identified PIFK-1, the orthologue of the
                      Drosophila PI 4-kinase four wheel drive (FWD), and found
                      that it is the only known factor so far that is essential
                      for the unfolded protein responses of both mitochondria and
                      endoplasmic reticulum. This suggests that both UPRs may
                      share a common membrane associated mechanism.},
      keywords     = {ATP-Binding Cassette Transporters: metabolism / Animals /
                      Caenorhabditis elegans: genetics / Caenorhabditis elegans:
                      growth $\&$ development / Caenorhabditis elegans: metabolism
                      / Caenorhabditis elegans Proteins: genetics / Caenorhabditis
                      elegans Proteins: metabolism / Cell Nucleus: genetics / Cell
                      Nucleus: metabolism / Endoplasmic Reticulum: genetics /
                      Endoplasmic Reticulum: metabolism / JNK Mitogen-Activated
                      Protein Kinases: genetics / JNK Mitogen-Activated Protein
                      Kinases: metabolism / Mitochondria: drug effects /
                      Mitochondria: metabolism / Molecular Chaperones / Paraquat:
                      pharmacology / Phosphorylation / Protein Folding / Reactive
                      Oxygen Species: metabolism / Reactive Oxygen Species:
                      toxicity / Signal Transduction: drug effects / Transcription
                      Factors: metabolism / Unfolded Protein Response: drug
                      effects / ATFS-1 protein, C elegans (NLM Chemicals) /
                      ATP-Binding Cassette Transporters (NLM Chemicals) /
                      Caenorhabditis elegans Proteins (NLM Chemicals) / HAF-1
                      protein, C elegans (NLM Chemicals) / Molecular Chaperones
                      (NLM Chemicals) / Reactive Oxygen Species (NLM Chemicals) /
                      Transcription Factors (NLM Chemicals) / JNK
                      Mitogen-Activated Protein Kinases (NLM Chemicals) / KGB-1
                      protein, C elegans (NLM Chemicals) / Paraquat (NLM
                      Chemicals)},
      cin          = {AG Vorberg},
      ddc          = {610},
      cid          = {I:(DE-2719)1013004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23516373},
      pmc          = {pmc:PMC3597513},
      doi          = {10.1371/journal.pgen.1003346},
      url          = {https://pub.dzne.de/record/141390},
}