Structural mechanisms of inflammasome regulation revealed by cryo-EM studies

被引：5
作者：
Cao, Jianhao [1 ]
Nash, Grady [1 ]
Zhang, Liman [1 ]
机构：
[1] Oregon Hlth & Sci Univ, Dept Chem Physiol & Biochem, Portland, OR 97239 USA
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 2022年 / 75卷
基金：
美国国家卫生研究院;
关键词：
NLRP3; INFLAMMASOME; FLAGELLIN; NEK7; RECOGNITION; ACTIVATION; PROTEIN;
D O I：
10.1016/j.sbi.2022.102390
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页数：8
相关论文
共 58 条
  • [1] NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation
    Andreeva, Liudmila
    David, Liron
    Rawson, Shaun
    Shen, Chen
    Pasricha, Teerithveen
    Pelegrin, Pablo
    Wu, Hao
    [J]. CELL, 2021, 184 (26) : 6299 - +
  • [2] Human NLRP1 is a sensor for double-stranded RNA
    Bauernfried, Stefan
    Scherr, Matthias J.
    Pichlmair, Andreas
    Duderstadt, Karl E.
    Hornung, Veit
    [J]. SCIENCE, 2021, 371 (6528) : 482 - +
  • [3] Inflammasomes: mechanism of assembly, regulation and signalling
    Broz, Petr
    Dixit, Vishva M.
    [J]. NATURE REVIEWS IMMUNOLOGY, 2016, 16 (07) : 407 - 420
  • [4] PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation
    Chen, Jueqi
    Chen, Zhijian J.
    [J]. NATURE, 2018, 564 (7734) : 71 - +
  • [5] N-terminal degradation activates the NLRP1B inflammasome
    Chui, Ashley J.
    Okondo, Marian C.
    Rao, Sahana D.
    Gai, Kuo
    Griswold, Andrew R.
    Johnson, Darren C.
    Ball, Daniel P.
    Taabazuing, Cornelius Y.
    Orth, Elizabeth L.
    Vittimberga, Brooke A.
    Bachovchin, Daniel A.
    [J]. SCIENCE, 2019, 364 (6435) : 82 - +
  • [6] A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases
    Coll, Rebecca C.
    Robertson, Avril A. B.
    Chae, Jae Jin
    Higgins, Sarah C.
    Munoz-Planillo, Raul
    Inserra, Marco C.
    Vetter, Irina
    Dungan, Lara S.
    Monks, Brian G.
    Stutz, Andrea
    Croker, Daniel E.
    Butler, Mark S.
    Haneklaus, Moritz
    Sutton, Caroline E.
    Nunez, Gabriel
    Latz, Eicke
    Kastner, Daniel L.
    Mills, Kingston H. G.
    Masters, Seth L.
    Schroder, Kate
    Cooper, Matthew A.
    O'Neill, Luke A. J.
    [J]. NATURE MEDICINE, 2015, 21 (03) : 248 - +
  • [7] de Olza MO, 2020, LANCET ONCOL, V21, pE419, DOI 10.1016/S1470-2045(20)30234-5
  • [8] Crystal Structure of NLRP3 NACHT Domain With an Inhibitor Defines Mechanism of Inflammasome Inhibition
    Dekker, Carien
    Mattes, Henri
    Wright, Michael
    Boettcher, Andreas
    Hinniger, Alexandra
    Hughes, Nicola
    Kapps-Fouthier, Sandra
    Eder, Jorg
    Erbel, Paulus
    Stiefl, Nikolaus
    Mackay, Angela
    Farady, Christopher J.
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2021, 433 (24)
  • [9] Autolytic Proteolysis within the Function to Find Domain (FIIND) Is Required for NLRP1 Inflammasome Activity
    Finger, Joshua N.
    Lich, John D.
    Dare, Lauren C.
    Cook, Michael N.
    Brown, Kristin K.
    Duraiswami, Chaya
    Bertin, John J.
    Gough, Peter J.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (30) : 25030 - 25037
  • [10] Proteolytic Processing of Nlrp1b Is Required for Inflammasome Activity
    Frew, Bradley C.
    Joag, Vineet R.
    Mogridge, Jeremy
    [J]. PLOS PATHOGENS, 2012, 8 (04)
123456