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@ARTICLE{Furthmann:1020576,
      author       = {Furthmann, Nikolas and Bader, Verian and Angersbach, Lena
                      and Blusch, Alina and Goel, Simran and Sánchez-Vicente, Ana
                      and Krause, Laura J. and Chaban, Sarah A. and Grover, Prerna
                      and Trinkaus, Victoria A. and van Well, Eva M. and
                      Jaugstetter, Maximilian and Tschulik, Kristina and Damgaard,
                      Rune Busk and Saft, Carsten and Ellrichmann, Gisa and Gold,
                      Ralf and Koch, Arend and Englert, Benjamin and Westenberger,
                      Ana and Klein, Christine and Jungbluth, Lisa and Sachse,
                      Carsten and Behrends, Christian and Glatzel, Markus and
                      Hartl, F. Ulrich and Nakamura, Ken and Christine, Chadwick
                      W. and Huang, Eric J. and Tatzelt, Jörg and Winklhofer,
                      Konstanze F.},
      title        = {{NEMO} reshapes the α-{S}ynuclein aggregate interface and
                      acts as an autophagy adapter by co-condensation with p62},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2024-00271},
      pages        = {8368},
      year         = {2023},
      abstract     = {NEMO is a ubiquitin-binding protein which regulates
                      canonical NF-κB pathwayactivation in innate immune
                      signaling, cell death regulation and
                      host-pathogeninteractions. Here we identify an
                      NF-κB-independent function of NEMO inproteostasis
                      regulation by promoting autophagosomal clearance of
                      proteinaggregates. NEMO-deficient cells accumulate misfolded
                      proteins upon proteotoxicstress and are vulnerable to
                      proteostasis challenges. Moreover, apatient with a mutation
                      in the NEMO-encoding IKBKG gene resulting indefective
                      binding of NEMO to linear ubiquitin chains, developed a
                      widespreadmixed brain proteinopathy, including α-synuclein,
                      tau and TDP-43 pathology.NEMO amplifies linear
                      ubiquitylation at α-synuclein aggregates and promotesthe
                      local concentration of p62 into foci. In vitro, NEMO lowers
                      the thresholdconcentrations required for ubiquitin-dependent
                      phase transition of p62. Insummary, NEMO reshapes the
                      aggregate surface for efficient
                      autophagosomalclearancebyprovidingamobilephase at
                      theaggregate interphase favoringcocondensationwith p62.},
      cin          = {ER-C-3 / IBI-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ER-C-3-20170113 / I:(DE-Juel1)IBI-6-20200312},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38114471},
      UT           = {WOS:001131904500002},
      doi          = {10.1038/s41467-023-44033-0},
      url          = {https://juser.fz-juelich.de/record/1020576},
}