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@ARTICLE{Wabnitz:137584,
      author       = {G. H. Wabnitz and H. Kirchgessner and B. Jahraus and L.
                      Umansky$^*$ and S. Shenolikar and Y. Samstag},
      title        = {{PP}1α and {C}ofilin regulate nuclear translocation of
                      {NF}k{B} and promote expression of the anti-inflammatory
                      cytokine {IL}-10 by {T}-cells.},
      journal      = {Molecular and cellular biology},
      volume       = {38},
      number       = {22},
      issn         = {1098-5549},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {DKFZ-2018-01464},
      pages        = {e00041-18},
      year         = {2018},
      abstract     = {While several protein serine-threonine kinases control
                      cytokine production by T-cells, the roles of
                      serine-threonine phosphatases are largely unexplored. Here,
                      we analysed the involvement of protein phosphatase-1α
                      (PP1α) in cytokine synthesis following costimulation of
                      primary human T-cells. SiRNA-mediated knock-down of PP1α
                      (PP1KD) or expression of a dominant-negative PP1α
                      (D95N-PP1) drastically diminished IL-10 production. Focusing
                      on a key transcriptional activator of human IL-10, we
                      demonstrate that nuclear translocation of NF-kB was
                      significantly inhibited in PP1KD or D95N-PP1 cells.
                      Interestingly, knockdown of cofilin, a known substrate of
                      PP1 containing a nuclear localization signal, also prevented
                      nuclear accumulation of NF-kB. Expression of a
                      constitutively active non-phosphorylatable S3A-cofilin in
                      D95N-PP1 cells restored nuclear translocation of NF-kB and
                      IL-10 expression. Sub-population analysis revealed that
                      defective nuclear translocation of NF-kB was most prominent
                      in CD4+CD45RA-CXCR3- T-cells that included IL-10-producing
                      TH2 cells. Together these findings reveal novel functions
                      for PP1α and its substrate cofilin in T-cells namely the
                      regulation of the nuclear translocation of NF-kB and
                      promotion of IL-10 production. These data suggest that
                      stimulation of PP1α could limit the overwhelming immune
                      responses seen in chronic inflammatory diseases.},
      cin          = {G808},
      ddc          = {570},
      cid          = {I:(DE-He78)G808-20160331},
      pnm          = {317 - Translational cancer research (POF3-317)},
      pid          = {G:(DE-HGF)POF3-317},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30181394},
      doi          = {10.1128/MCB.00041-18},
      url          = {https://inrepo02.dkfz.de/record/137584},
}