Publication: ASC oligomer favors caspase-1CARD domain recruitment after intracellular potassium efflux
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Date
2023-07-04
Authors
Martín Sánchez, María Rosario Fátima ; Compan, Vincent ; Peñín Franch, Alejandro ; Tapia Abellán, Ana ; Gómez, Ana I. ; Baños Gregori, María C. ; Schmidt, Florian I. ; Pelegrín Vivancos, Pablo
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Publisher
Rockefeller University Press
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DOI
https://doi.org/10.1083/jcb.202003053
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info:eu-repo/semantics/article
Description
Abstract
Signaling 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.
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Citation
J Cell Biol (2023) 222 (8): e202003053
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