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@ARTICLE{Liess:425979,
      author       = {Liess, Anna K. L. and Kucerova, Alena and Schweimer,
                      Kristian and Yu, Lu and Roumeliotis, Theodoros I. and
                      Diebold, Mathias and Dybkov, Olexandr and Sotriffer,
                      Christoph and Urlaub, Henning and Choudhary, Jyoti S. and
                      Mansfeld, Jörg and Lorenz, Sonja},
      title        = {{A}utoinhibition {M}echanism of the
                      {U}biquitin-{C}onjugating {E}nzyme {UBE}2{S} by
                      {A}utoubiquitination},
      journal      = {Structure},
      volume       = {27},
      number       = {8},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {PUBDB-2019-03522},
      pages        = {1195 - 1210.e7},
      year         = {2019},
      note         = {© Elsevier Ltd.; Post referee fulltext in progress;
                      Embargo 12 months from publication},
      abstract     = {Ubiquitin-conjugating enzymes (E2s) govern key aspects of
                      ubiquitin signaling. Emerging evidence suggests that the
                      activities of E2s are modulated by posttranslational
                      modifications; the structural underpinnings, however, are
                      largely unclear. Here, we unravel the structural basis and
                      mechanistic consequences of a conserved autoubiquitination
                      event near the catalytic center of E2s, using the human
                      anaphase-promoting complex/cyclosome-associated UBE2S as a
                      model system. Crystal structures we determined of the
                      catalytic ubiquitin carrier protein domain combined with MD
                      simulations reveal that the active-site region is malleable,
                      which permits an adjacent ubiquitin acceptor site,
                      Lys$^{+5}$, to be ubiquitinated intramolecularly. We
                      demonstrate by NMR that the Lys$^{+5}$-linked ubiquitin
                      inhibits UBE2S by obstructing its reloading with ubiquitin.
                      By immunoprecipitation, quantitative mass spectrometry, and
                      siRNA-and-rescue experiments we show that Lys$^{+5}$
                      ubiquitination of UBE2S decreases during mitotic exit but
                      does not influence proteasomal turnover of this E2. These
                      findings suggest that UBE2S activity underlies inherent
                      regulation during the cell cycle.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31230944},
      UT           = {WOS:000478962400005},
      doi          = {10.1016/j.str.2019.05.008},
      url          = {https://bib-pubdb1.desy.de/record/425979},
}