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@ARTICLE{Chen:303258,
      author       = {W. W. Chen and T. A. Rodrigues and D. Wendscheck and A. G.
                      Pedrosa and C. Yang and T. Francisco and T.
                      Möcklinghoff$^*$ and A. Zografakis and B. Nunes-Silva and
                      R. E. Avraham and A. R. Silva and M. J. Ferreira and H. Das
                      and J. Koster and S. Neuwirth and J. Bender and S.
                      Oeljeklaus and V. Sondhi and C. Gatsogiannis and M.
                      Schuldiner and E. Zalckvar and K. Hofmann and H. R. Waterham
                      and R. J. DeBerardinis and J. E. Azevedo and B. Warscheid},
      title        = {{PEX}39 facilitates the peroxisomal import of
                      {PTS}2-containing proteins.},
      journal      = {Nature cell biology},
      volume       = {27},
      number       = {8},
      issn         = {1465-7392},
      address      = {New York, NY},
      publisher    = {Nature America},
      reportid     = {DKFZ-2025-01603},
      pages        = {1256-1271},
      year         = {2025},
      note         = {2025 Aug;27(8):1256-1271},
      abstract     = {Peroxisomes are metabolic organelles essential for human
                      health. Defects in peroxisomal biogenesis proteins (also
                      known as peroxins (PEXs)) cause devastating disease. PEX7
                      binds proteins containing a type 2 peroxisomal targeting
                      signal (PTS2) to enable their import from the cytosol into
                      peroxisomes, although many aspects of this process remain
                      enigmatic. Utilizing in vitro assays, yeast and human cells,
                      we show that PEX39, a previously uncharacterized protein, is
                      a cytosolic peroxin that facilitates the import of
                      PTS2-containing proteins by binding PEX7 and stabilizing its
                      interaction with cargo proteins containing a PTS2. PEX39 and
                      PEX13, a peroxisomal membrane translocon protein, both
                      possess an (R/K)PWE motif necessary for PEX7 binding.
                      Handover of PEX7 from PEX39 to PEX13 via these motifs
                      provides a new paradigm for peroxisomal protein import and
                      biogenesis. Collectively, this work reveals how PEX39 and
                      (R/K)PWE motifs facilitate the import of PTS2-containing
                      proteins and advances our understanding of peroxisomal
                      disease.},
      cin          = {B200},
      ddc          = {570},
      cid          = {I:(DE-He78)B200-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40739340},
      doi          = {10.1038/s41556-025-01711-z},
      url          = {https://inrepo02.dkfz.de/record/303258},
}