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@ARTICLE{Oroz:138760,
      author       = {Oroz, Javier and Barrera-Vilarmau, Susana and Alfonso,
                      Carlos and Rivas, Germán and de Alba, Eva},
      title        = {{ASC} {P}yrin {D}omain {S}elf-associates and {B}inds
                      {NLRP}3 {P}rotein {U}sing {E}quivalent {B}inding
                      {I}nterfaces.},
      journal      = {The journal of biological chemistry},
      volume       = {291},
      number       = {37},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.60645},
      reportid     = {DZNE-2020-05082},
      pages        = {19487-19501},
      year         = {2016},
      abstract     = {Death domain superfamily members typically act as adaptors
                      mediating in the assembly of supramolecular complexes with
                      critical apoptosis and inflammation functions. These modular
                      proteins consist of death domains, death effector domains,
                      caspase recruitment domains, and pyrin domains (PYD).
                      Despite the high structural similarity among them, only
                      homotypic interactions participate in complex formation,
                      suggesting that subtle factors differentiate each
                      interaction type. It is thus critical to identify these
                      factors as an essential step toward the understanding of the
                      molecular basis of apoptosis and inflammation. The proteins
                      apoptosis-associated speck-like protein containing a CARD
                      (ASC) and NLRP3 play key roles in the regulation of
                      apoptosis and inflammation through self-association and
                      protein-protein interactions mediated by their PYDs. To
                      better understand the molecular basis of their function, we
                      have characterized ASC and NLRP3 PYD self-association and
                      their intermolecular interaction by solution NMR
                      spectroscopy and analytical ultracentrifugation. We found
                      that ASC self-associates and binds NLRP3 PYD through
                      equivalent protein regions, with higher binding affinity for
                      the latter. These regions are located at opposite sides of
                      the protein allowing multimeric complex formation previously
                      shown in ASC PYD fibril assemblies. We show that NLRP3 PYD
                      coexists in solution as a monomer and highly populated
                      large-order oligomerized species. Despite this, we
                      determined its monomeric three-dimensional solution
                      structure by NMR and characterized its binding to ASC PYD.
                      Using our novel structural data, we propose molecular models
                      of ASC·ASC and ASC·NLRP3 PYD early supramolecular
                      complexes, providing new insights into the molecular
                      mechanisms of inflammasome and apoptosis signaling.},
      keywords     = {CARD Signaling Adaptor Proteins / Cytoskeletal Proteins:
                      chemistry / Cytoskeletal Proteins: genetics / Cytoskeletal
                      Proteins: metabolism / Humans / Models, Molecular / NLR
                      Family, Pyrin Domain-Containing 3 Protein: chemistry / NLR
                      Family, Pyrin Domain-Containing 3 Protein: genetics / NLR
                      Family, Pyrin Domain-Containing 3 Protein: metabolism /
                      Nuclear Magnetic Resonance, Biomolecular / Protein Binding /
                      Protein Structure, Quaternary / Pyrin Domain /
                      Ultracentrifugation / CARD Signaling Adaptor Proteins (NLM
                      Chemicals) / Cytoskeletal Proteins (NLM Chemicals) / NLR
                      Family, Pyrin Domain-Containing 3 Protein (NLM Chemicals) /
                      NLRP3 protein, human (NLM Chemicals) / PYCARD protein, human
                      (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {540},
      cid          = {I:(DE-2719)1410001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27432880},
      pmc          = {pmc:PMC5016686},
      doi          = {10.1074/jbc.M116.741082},
      url          = {https://pub.dzne.de/record/138760},
}