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@ARTICLE{Herrera:1050651,
      author       = {Herrera, Maria G. and Kühn, Lena and Jungbluth, Lisa and
                      Bader, Verian and Krause, Laura J. and Kartte, David and
                      Adriaenssens, Elias and Martens, Sascha and Tatzelt, Jörg
                      and Sachse, Carsten and Winklhofer, Konstanze F.},
      title        = {{TBK}1 {I}nduces the {F}ormation of {O}ptineurin
                      {F}ilaments {T}hat {C}ondensate with {P}olyubiquitin and
                      {LC}3 for {C}argo {S}equestration},
      journal      = {Advanced science},
      volume       = {1},
      issn         = {2198-3844},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2026-00403},
      pages        = {e09927},
      year         = {2025},
      abstract     = {Optineurin is an autophagy receptor that plays an important
                      role in the selective degradation of mitochondria, protein
                      aggregates, and intracellular pathogens. It recognizes
                      ubiquitylated cargo by its ubiquitin-binding in ABIN and
                      NEMO (UBAN) domain and recruits the autophagic machinery
                      through its LC3-interacting region (LIR) domain.
                      Phosphorylation of Optineurin by TANK-binding kinase 1
                      (TBK1) increases the binding of Optineurin to both ubiquitin
                      chains and lipidated microtubule-associated protein light
                      chain 3 (LC3). Optineurin has been reported to form foci at
                      ubiquitylated cargo, but the underlying mechanism and how
                      these foci are linked to selective autophagy has remained
                      largely unknown. This study shows that phosphorylation of
                      Optineurin by TBK1 induces the formation of filaments that
                      phase separate upon binding to linear polyubiquitin. LC3
                      anchored to unilamellar vesicles co-partitions into
                      Optineurin/polyubiquitin condensates, resulting in the local
                      deformation of the vesicle membrane. Thus, the condensation
                      of filamentous Optineurin with ubiquitylated cargo promotes
                      the nucleation of cargo and its subsequent alignment with
                      LC3-positive nascent autophagosomes, suggesting that
                      co-condensation processes ensure directionality in selective
                      autophagy.},
      cin          = {ER-C-3},
      ddc          = {624},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      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},
      doi          = {10.1002/advs.202509927},
      url          = {https://juser.fz-juelich.de/record/1050651},
}