TY - JOUR
T1 - Structural mechanisms of inflammasome regulation revealed by cryo-EM studies
AU - Cao, Jianhao
AU - Nash, Grady
AU - Zhang, Liman
N1 - Publisher Copyright:
© 2022 Elsevier Ltd
PY - 2022/8
Y1 - 2022/8
N2 - Inflammasomes are cytosolic protein complexes that form in response to pathogen or damage signals and initiate inflammation. Signal transduction in the inflammasome pathway occurs via protein–protein interaction, protein conformational change, and oligomerization. Recent advances in structural biology have provided multiple insights in inflammasome regulation that are both biologically intriguing and therapeutically valuable. In this review, we summarize the current understanding of three most studied inflammasome complexes: the NAIP/NLRC4, NLRP1, and NLRP3 inflammasomes. We discuss the general mechanisms and unique features of their regulation and how investigating these systems may contribute to therapeutic applications.
AB - Inflammasomes are cytosolic protein complexes that form in response to pathogen or damage signals and initiate inflammation. Signal transduction in the inflammasome pathway occurs via protein–protein interaction, protein conformational change, and oligomerization. Recent advances in structural biology have provided multiple insights in inflammasome regulation that are both biologically intriguing and therapeutically valuable. In this review, we summarize the current understanding of three most studied inflammasome complexes: the NAIP/NLRC4, NLRP1, and NLRP3 inflammasomes. We discuss the general mechanisms and unique features of their regulation and how investigating these systems may contribute to therapeutic applications.
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U2 - 10.1016/j.sbi.2022.102390
DO - 10.1016/j.sbi.2022.102390
M3 - Review article
C2 - 35636002
AN - SCOPUS:85130910511
SN - 0959-440X
VL - 75
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
M1 - 102390
ER -