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@ARTICLE{Busch:155695,
      author       = {Busch, Julia and Moreno, Rita and de la Vega, Laureano and
                      Saul, Vera Vivian and Bacher, Susanne and Zweydorf, Felix
                      and Ueffing, Marius and Weber, Axel and Gloeckner, Christian
                      Johannes and Linne, Uwe and Kracht, Michael and Schmitz,
                      Michael Lienhard},
      title        = {{TRAF}6 {P}hosphorylation {P}revents {I}ts {A}utophagic
                      {D}egradation and {R}e-{S}hapes {LPS}-{T}riggered
                      {S}ignaling {N}etworks.},
      journal      = {Cancers},
      volume       = {13},
      number       = {14},
      issn         = {2072-6694},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {DZNE-2021-00863},
      pages        = {3618},
      year         = {2021},
      abstract     = {The ubiquitin E3 ligase TNF Receptor Associated Factor 6
                      (TRAF6) participates in a large number of different
                      biological processes including innate immunity,
                      differentiation and cell survival, raising the need to
                      specify and shape the signaling output. Here, we identify a
                      lipopolysaccharide (LPS)-dependent increase in TRAF6
                      association with the kinase IKKε (inhibitor of NF-κB
                      kinase subunit ε) and IKKε-mediated TRAF6 phosphorylation
                      at five residues. The reconstitution of TRAF6-deficient
                      cells, with TRAF6 mutants representing
                      phosphorylation-defective or phospho-mimetic TRAF6 variants,
                      showed that the phospho-mimetic TRAF6 variant was largely
                      protected from basal ubiquitin/proteasome-mediated
                      degradation, and also from autophagy-mediated decay in
                      autolysosomes induced by metabolic perturbation. In
                      addition, phosphorylation of TRAF6 and its E3 ligase
                      function differentially shape basal and LPS-triggered
                      signaling networks, as revealed by phosphoproteome analysis.
                      Changes in LPS-triggered phosphorylation networks of cells
                      that had experienced autophagy are partially dependent on
                      TRAF6 and its phosphorylation status, suggesting an
                      involvement of this E3 ligase in the interplay between
                      metabolic and inflammatory circuits.},
      keywords     = {IKKε (Other) / LPS (Other) / NF-κB (Other) / TRAF6
                      (Other) / autophagy (Other) / kinase activation (Other) /
                      phosphorylation (Other) / signaling (Other)},
      cin          = {AG Gloeckner},
      ddc          = {610},
      cid          = {I:(DE-2719)1210007},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34298830},
      pmc          = {pmc:PMC8303406},
      doi          = {10.3390/cancers13143618},
      url          = {https://pub.dzne.de/record/155695},
}