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

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dc.contributor.authorMartín Sánchez, María Rosario Fátima
dc.contributor.authorCompan, Vincent
dc.contributor.authorPeñín Franch, Alejandro
dc.contributor.authorTapia Abellán, Ana
dc.contributor.authorGómez, Ana I.
dc.contributor.authorBaños Gregori, María C.
dc.contributor.authorSchmidt, Florian I.
dc.contributor.authorPelegrín Vivancos, Pablo
dc.contributor.departmentFarmacología
dc.date.accessioned2026-02-26T15:11:48Z
dc.date.available2026-02-26T15:11:48Z
dc.date.copyright© 2023 Martín Sánchez et al.
dc.date.issued2023-07-04
dc.description.abstractSignaling through the inflammasome is important for the inflammatory response. Low concentrations of intracellular K+ areassociated with the specific oligomerization and activation of the NLRP3 inflammasome, a type of inflammasome involved insterile inflammation. After NLRP3 oligomerization, ASC protein binds and forms oligomeric filaments that culminate in largeprotein 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 respectivecaspase activation and recruitment domains (CARD). So far, ASC oligomerization and caspase-1 activation are K+-independentprocesses. Here, we found that when there is low intracellular K+, ASC oligomers change their structure independently ofNLRP3 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 the pro-caspase-1 CARD domain into the ASC specks.
dc.formatapplication/pdf
dc.format.extent17
dc.identifier.citationJ Cell Biol (2023) 222 (8): e202003053
dc.identifier.doihttps://doi.org/10.1083/jcb.202003053
dc.identifier.eissn1540-8140
dc.identifier.issn0021-9525
dc.identifier.urihttp://hdl.handle.net/10201/214861
dc.languageeng
dc.publisherRockefeller University Press
dc.relationEste trabajo ha sido financiado por: • MCIN/AEI/10.13039/501100011033 (proyecto PID2020-116709RB-I00). • Ministerio de Economía, Industria y Competitividad–Fondo Europeo de Desarrollo Regional (proyecto SAF2017-88276-R). • Fundación Séneca (proyectos 20859/PI/18 y 21897/PI/22). • European Research Council (ERC-2013-CoG nº 614578 y ERC-2019-PoC nº 899636). • Instituto de Salud Carlos III (proyecto DTS21/00080). • UE Horizon 2020, proyecto PlasticHeal (grant 965196). • Deutsche Forschungsgemeinschaft (DFG) a través del programa Emmy Noether (SCHM 33361-1) y Germany’s Excellence Strategy–EXC2151–390873048 (para F.I. Schmidt)
dc.relation.publisherversionhttps://rupress.org/jcb/article/222/8/e202003053/214211/ASC-oligomer-favors-caspase-1CARD-domain
dc.rightsAttribution 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.odsObjetivo 3: Salud
dc.titleASC oligomer favors caspase-1CARD domain recruitment after intracellular potassium efflux
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublicationes
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relation.isAuthorOfPublication547c4c2c-d906-4e1d-ae9a-0cdb40eef6d1
relation.isAuthorOfPublication.latestForDiscoveryeefc2e40-b110-47b5-a081-bcf37256af4c
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