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@ARTICLE{UkmarGodec:153283,
      author       = {Ukmar-Godec, Tina and Fang, P. and Ibanez de Opakua, Alain
                      and Henneberg, F. and Godec, A. and Pan, K.-T. and Cima
                      Omori, Maria Sol and Chari, A. and Mandelkow, Eckhard and
                      Urlaub, H. and Zweckstetter, Markus},
      title        = {{P}roteasomal degradation of the intrinsically disordered
                      protein tau at single-residue resolution},
      journal      = {Science advances},
      volume       = {6},
      number       = {30},
      issn         = {2375-2548},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {DZNE-2020-01280},
      pages        = {eaba3916 -},
      year         = {2020},
      abstract     = {Intrinsically disordered proteins (IDPs) can be degraded in
                      a ubiquitin-independent process by the 20S proteasome.
                      Decline in 20S activity characterizes neurodegenerative
                      diseases. Here, we examine 20S degradation of IDP tau, a
                      protein that aggregates into insoluble deposits in
                      Alzheimer’s disease. We show that cleavage of tau by the
                      20S proteasome is most efficient within the
                      aggregation-prone repeat region of tau and generates both
                      short, aggregation-deficient peptides and two long fragments
                      containing residues 1 to 251 and 1 to 218. Phosphorylation
                      of tau by the non-proline–directed
                      Ca2+/calmodulin-dependent protein kinase II inhibits
                      degradation by the 20S proteasome. Phosphorylation of tau by
                      GSK3β, a major proline-directed tau kinase, modulates tau
                      degradation kinetics in a residue-specific manner. The study
                      provides detailed insights into the degradation products of
                      tau generated by the 20S proteasome, the residue specificity
                      of degradation, single-residue degradation kinetics, and
                      their regulation by posttranslational modification.},
      cin          = {Göttingen common / AG Zweckstetter / AG Mandelkow 1},
      ddc          = {500},
      cid          = {I:(DE-2719)6000014 / I:(DE-2719)1410001 /
                      I:(DE-2719)1013014},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC7439447},
      pubmed       = {pmid:32832664},
      doi          = {10.1126/sciadv.aba3916},
      url          = {https://pub.dzne.de/record/153283},
}