Mistargeting of hydrophobic mitochondrial proteins activates a nucleus-mediated posttranscriptional quality control pathway in trypanosomes
Dewar, C. E.; Oeljeklaus, S.; Mani, J.; Mühlhäuser, W. W. D.; Warscheid, B.; Schneider, A.
Show abstract
Mitochondrial protein import in the parasitic protozoan Trypanosoma brucei is mediated by the atypical outer membrane translocase, ATOM. It consists of seven subunits including ATOM69, the import receptor for hydrophobic proteins. Ablation of ATOM69, but not of any other subunit, triggers a unique quality control pathway resulting in the proteasomal degradation of non-imported mitochondrial proteins. The process requires a protein of unknown function, an E3 ubiquitin ligase and the ubiquitin-like protein (TbUbL1), which all are recruited to the mitochondrion upon ATOM69 depletion. TbUbL1 is a nuclear protein, a fraction of which is released to the cytosol upon triggering of the pathway. Nuclear release is essential as cytosolic TbUbL1 can bind mislocalised mitochondrial proteins and likely transfers them to the proteasome. Mitochondrial quality control has previously been studied in yeast and metazoans. Finding such a pathway in the highly diverged trypanosomes suggests such pathways are an obligate feature of all mitochondria.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- The Flemmingsome reveals an ESCRT-to-membrane coupling required for completion of cytokinesis 95%
- GAK and PRKCD are positive regulators of PRKN-independent mitophagy 95%
- The ubiquitin ligase Hecw controls oogenesis and neuronal homeostasis by promoting the liquid state of ribonucleoprotein particles 94%
Similar papers in this journal
Similar papers in this journal
- Increased levels of the mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol 94%
- MitoStores: Chaperone-controlled protein granules store mitochondrial precursors in the cytosol 94%
- Activation of goblet cell stress sensor IRE1β is controlled by the mucin chaperone AGR2 93%
Similar papers in this journal
- ATAD1 and the integrated stress response prevent clogging of TOM and damage caused by un-imported mitochondrial proteins 95%
- The E3 ubiquitin ligase FBXL6 controls the quality of newly synthesized mitochondrial ribosomal proteins 95%
- ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct 95%
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.