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@ARTICLE{Hoffmann:283176,
      author       = {Hoffmann, Christian and Nagao, Takahiro and Tsunoyama, Taka
                      A and Tromm, Johannes Vincent and Logan, Chinyere and
                      Nakamura, Koki and Wang, Han and Bianchi, Frans and van den
                      Bogaart, Geert and Kusumi, Akihiro and Hirabayashi, Yusuke
                      and Milovanovic, Dragomir},
      title        = {{M}embrane-protein-mediated phase separation orchestrates
                      organelle contact sites.},
      journal      = {Molecular cell},
      volume       = {86},
      number       = {1},
      issn         = {1097-2765},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {DZNE-2026-00055},
      pages        = {135 - 149.e9},
      year         = {2026},
      abstract     = {Mitochondria and the endoplasmic reticulum (ER) contain
                      large areas that are in close proximity. Yet the mechanism
                      of how these inter-organellar adhesions are formed remains
                      elusive. Tight functional connections, termed 'membrane
                      contact sites,' assemble at these areas and are essential
                      for exchanging metabolites and lipids between the
                      organelles. Recently, the ER-resident protein PDZ
                      domain-containing protein 8 (PDZD8) was identified as a
                      tether between the ER and mitochondria or late
                      endosomes/lysosomes. Here, we show that PDZD8 can undergo
                      phase separation via its intrinsically disordered region
                      (IDR). Endogenously labeled PDZD8 forms condensates on
                      membranes both in vitro and in mammalian cells. Electron
                      microscopy analyses indicate that the expression of
                      full-length PDZD8 rescues the decrease in inter-organelle
                      contacts in PDZD8 knockout cells but not PDZD8 lacking its
                      IDR. Together, this study identifies that PDZD8 condensates
                      at the lipid interfaces act as an adhesive framework that
                      stitches together the neighboring organelles and supports
                      the structural and functional integrity of inter-organelle
                      communication.},
      keywords     = {Humans / Endoplasmic Reticulum: metabolism / Endoplasmic
                      Reticulum: ultrastructure / Endoplasmic Reticulum: genetics
                      / Mitochondria: metabolism / Mitochondria: ultrastructure /
                      Mitochondria: genetics / Membrane Proteins: metabolism /
                      Membrane Proteins: genetics / Membrane Proteins: chemistry /
                      HeLa Cells / HEK293 Cells / Animals / Intrinsically
                      Disordered Proteins: metabolism / Intrinsically Disordered
                      Proteins: genetics / Biomolecular Condensates: metabolism /
                      Phase Separation / PDZD8 (Other) / biomolecular condensates
                      (Other) / endoplasmic reticulum (Other) / liquid-liquid
                      phase separation (Other) / membrane contact sites (Other) /
                      mitochondria (Other) / Membrane Proteins (NLM Chemicals) /
                      Intrinsically Disordered Proteins (NLM Chemicals)},
      cin          = {AG Milovanovic (Berlin)},
      ddc          = {610},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41512824},
      doi          = {10.1016/j.molcel.2025.12.006},
      url          = {https://pub.dzne.de/record/283176},
}