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@ARTICLE{Roiuk:292099,
      author       = {M. Roiuk$^*$ and M. Neff$^*$ and A. Teleman$^*$},
      title        = {e{IF}4{E}-independent translation is largely
                      e{IF}3d-dependent.},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DKFZ-2024-01598},
      pages        = {6692},
      year         = {2024},
      note         = {#EA:B140#LA:B140#},
      abstract     = {Translation initiation is a highly regulated step needed
                      for protein synthesis. Most cell-based mechanistic work on
                      translation initiation has been done using non-stressed
                      cells growing in medium with sufficient nutrients and
                      oxygen. This has yielded our current understanding of
                      'canonical' translation initiation, involving recognition of
                      the mRNA cap by eIF4E1 followed by successive recruitment of
                      initiation factors and the ribosome. Many cells, however,
                      such as tumor cells, are exposed to stresses such as
                      hypoxia, low nutrients or proteotoxic stress. This leads to
                      inactivation of mTORC1 and thereby inactivation of eIF4E1.
                      Hence the question arises how cells translate mRNAs under
                      such stress conditions. We study here how mRNAs are
                      translated in an eIF4E1-independent manner by blocking
                      eIF4E1 using a constitutively active version of
                      eIF4E-binding protein (4E-BP). Via ribosome profiling we
                      identify a subset of mRNAs that are still efficiently
                      translated when eIF4E1 is inactive. We find that these mRNAs
                      preferentially release eIF4E1 when eIF4E1 is inactive and
                      bind instead to eIF3d via its cap-binding pocket. eIF3d then
                      enables these mRNAs to be efficiently translated due to its
                      cap-binding activity. In sum, our work identifies
                      eIF3d-dependent translation as a major mechanism enabling
                      mRNA translation in an eIF4E-independent manner.},
      keywords     = {Eukaryotic Initiation Factor-4E: metabolism / Eukaryotic
                      Initiation Factor-4E: genetics / Eukaryotic Initiation
                      Factor-3: metabolism / Eukaryotic Initiation Factor-3:
                      genetics / Humans / RNA, Messenger: metabolism / RNA,
                      Messenger: genetics / Protein Biosynthesis / Ribosomes:
                      metabolism / Protein Binding / RNA Caps: metabolism / HEK293
                      Cells / Peptide Chain Initiation, Translational / Cell Cycle
                      Proteins / Adaptor Proteins, Signal Transducing / Eukaryotic
                      Initiation Factor-4E (NLM Chemicals) / Eukaryotic Initiation
                      Factor-3 (NLM Chemicals) / RNA, Messenger (NLM Chemicals) /
                      EIF3D protein, human (NLM Chemicals) / EIF4E protein, human
                      (NLM Chemicals) / RNA Caps (NLM Chemicals) / EIF4EBP1
                      protein, human (NLM Chemicals) / Cell Cycle Proteins (NLM
                      Chemicals) / Adaptor Proteins, Signal Transducing (NLM
                      Chemicals)},
      cin          = {B140},
      ddc          = {500},
      cid          = {I:(DE-He78)B140-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39107322},
      doi          = {10.1038/s41467-024-51027-z},
      url          = {https://inrepo02.dkfz.de/record/292099},
}