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@ARTICLE{Stutz:139309,
      author       = {Stutz, Andrea and Kolbe, Carl-Christian and Stahl, Rainer
                      and Horvath, Gabor L and Franklin, Bernardo S and van Ray,
                      Olivia and Brinkschulte, Rebecca and Geyer, Matthias and
                      Meissner, Felix and Latz, Eicke},
      title        = {{NLRP}3 inflammasome assembly is regulated by
                      phosphorylation of the pyrin domain.},
      journal      = {Journal of experimental medicine},
      volume       = {214},
      number       = {6},
      issn         = {0022-1007},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {DZNE-2020-05631},
      pages        = {1725-1736},
      year         = {2017},
      abstract     = {NLRP3 is a cytosolic pattern recognition receptor that
                      senses microbes and endogenous danger signals. Upon
                      activation, NLRP3 forms an inflammasome with the adapter
                      ASC, resulting in caspase-1 activation, release of
                      proinflammatory cytokines and cell death. How NLRP3
                      activation is regulated by transcriptional and
                      posttranslational mechanisms to prevent aberrant activation
                      remains incompletely understood. Here, we identify three
                      conserved phosphorylation sites in NLRP3 and demonstrate
                      that NLRP3 activation is controlled by phosphorylation of
                      its pyrin domain (PYD). Phosphomimetic residues in NLRP3 PYD
                      abrogate inflammasome activation and structural modeling
                      indicates that phosphorylation of the PYD regulates
                      charge-charge interaction between two PYDs that are
                      essential for NLRP3 activation. Phosphatase 2A (PP2A)
                      inhibition or knock-down drastically reduces NLRP3
                      activation, showing that PP2A can license inflammasome
                      assembly via dephosphorylating NLRP3 PYD. These results
                      propose that the balance between kinases and phosphatases
                      acting on the NLRP3 PYD is critical for NLRP3 activation.},
      keywords     = {Amino Acid Sequence / Animals / HEK293 Cells / Humans /
                      Inflammasomes: metabolism / Mice / Models, Biological /
                      Models, Molecular / NLR Family, Pyrin Domain-Containing 3
                      Protein: chemistry / NLR Family, Pyrin Domain-Containing 3
                      Protein: metabolism / Phosphorylation / Phosphoserine:
                      metabolism / Protein Binding / Protein Domains / Protein
                      Phosphatase 2: metabolism / Pyrin: chemistry /
                      Structure-Activity Relationship / Inflammasomes (NLM
                      Chemicals) / NLR Family, Pyrin Domain-Containing 3 Protein
                      (NLM Chemicals) / Nlrp3 protein, mouse (NLM Chemicals) /
                      Pyrin (NLM Chemicals) / Phosphoserine (NLM Chemicals) /
                      Protein Phosphatase 2 (NLM Chemicals)},
      cin          = {AG Latz},
      ddc          = {610},
      cid          = {I:(DE-2719)1013024},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28465465},
      pmc          = {pmc:PMC5460996},
      doi          = {10.1084/jem.20160933},
      url          = {https://pub.dzne.de/record/139309},
}