Data for: ASC oligomer favors caspase-1 CARD domain recruitment after intracellular potassium efflux

  1. Martín-Sánchez, Fátima 1
  2. Compan, Vincent 2
  3. Peñín-Franch, Alejandro 1
  4. Tapia-Abellán, Ana 1
  5. Gómez, Ana I 1
  6. Baños, Maria C 1
  7. Schmidt, Florian I. 3
  8. Pelegrin, Pablo 4
  1. 1 Biomedical research institute of Murcia
  2. 2 University of Montpellier
    info

    University of Montpellier

    Montpellier, Francia

    ROR https://ror.org/051escj72

  3. 3 University of Bonn
    info

    University of Bonn

    Bonn, Alemania

    ROR https://ror.org/041nas322

  4. 4 Universidad de Murcia
    info

    Universidad de Murcia

    Murcia, España

    ROR https://ror.org/03p3aeb86

Mostrar afiliacións +

Editor: Dryad

Ano de publicación: 2023

Tipo: Dataset

CC0 1.0

DOI: 10.5061/DRYAD.N8PK0P31B lock_openAcceso aberto editor

Resumo

Signaling through the inflammasome is important for the inflammatory response. Low concentrations of intracellular K+are associated with the specific oligomerization and activation of the NLRP3 inflammasome, a type of inflammasome involved in sterile inflammation. After NLRP3 oligomerization, ASC protein binds and forms oligomeric filaments that culminate in large protein complexes named ASC specks. ASC specks are also initiated from different inflammasome scaffolds, such as AIM2, NLRC4 or Pyrin. ASC oligomers recruit caspase-1 and then induce its activation through interactions between their respective caspase activation and recruitment domains (CARD). So far ASC oligomerization and caspase-1 activation are K+-independent processes. Here we found that, when there is low intracellular K+, ASC oligomers change their structure independently of NLRP3 and make the ASCCARD domain more accessible for the recruitment of the pro-caspase-1CARD domain. Therefore, conditions that decrease intracellular K+ not only drive NLRP3 responses but also enhance the recruitment of pro-caspase-1 CARD domain into the ASC specks.