PMID- 27139490
OWN - NLM
STAT- MEDLINE
DCOM- 20170721
LR  - 20181113
IS  - 1540-9538 (Electronic)
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 213
IP  - 6
DP  - 2016 May 30
TI  - NLRP3 recruitment by NLRC4 during Salmonella infection.
PG  - 877-85
LID - 10.1084/jem.20132234 [doi]
AB  - NLRC4 and NLRP3, of the NOD-like receptor (NLR) family of intracellular proteins, 
      are expressed in innate immune cells and are thought to nucleate distinct 
      inflammasome complexes that promote caspase-1 activation, secretion of the 
      proinflammatory cytokines IL-1beta and IL-18, and a form of cell death termed 
      pyroptosis. We show that NLRP3 associates with NLRC4 in macrophages infected with 
      Salmonella typhimurium or transfected with flagellin. The significance of the 
      interaction between the NLRC4 NACHT domain and NLRP3 was revealed when 
      Nlrc4(S533A/S533A) bone marrow-derived macrophages (BMDMs) expressing 
      phosphorylation site mutant NLRC4 S533A had only a mild defect in caspase-1 
      activation when compared with NLRC4-deficient BMDMs. NLRC4 S533A activated 
      caspase-1 by recruiting NLRP3 and its adaptor protein ASC. Thus, 
      Nlrc4(S533A/S533A) Nlrp3(-/-) BMDMs more closely resembled Nlrc4(-/-) BMDMs in 
      their response to S. typhimurium or flagellin. The interplay between NLRP3 and 
      NLRC4 reveals an unexpected overlap between what had been considered distinct 
      inflammasome scaffolds.
CI  - (c) 2016 Qu et al.
FAU - Qu, Yan
AU  - Qu Y
AD  - Department of Physiological Chemistry, Genentech Inc., South San Francisco, CA 
      94080.
FAU - Misaghi, Shahram
AU  - Misaghi S
AD  - Department of Early Stage Cell Culture, Genentech Inc., South San Francisco, CA 
      94080.
FAU - Newton, Kim
AU  - Newton K
AD  - Department of Physiological Chemistry, Genentech Inc., South San Francisco, CA 
      94080.
FAU - Maltzman, Allie
AU  - Maltzman A
AD  - Department of Physiological Chemistry, Genentech Inc., South San Francisco, CA 
      94080.
FAU - Izrael-Tomasevic, Anita
AU  - Izrael-Tomasevic A
AD  - Department of Protein Chemistry, Genentech Inc., South San Francisco, CA 94080.
FAU - Arnott, David
AU  - Arnott D
AD  - Department of Protein Chemistry, Genentech Inc., South San Francisco, CA 94080.
FAU - Dixit, Vishva M
AU  - Dixit VM
AD  - Department of Physiological Chemistry, Genentech Inc., South San Francisco, CA 
      94080 dixit@gene.com.
LA  - eng
PT  - Journal Article
DEP - 20160502
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Apoptosis Regulatory Proteins)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Ipaf protein, mouse)
RN  - 0 (NLR Family, Pyrin Domain-Containing 3 Protein)
RN  - 0 (Nlrp3 protein, mouse)
RN  - 12777-81-0 (Flagellin)
SB  - IM
MH  - Amino Acid Substitution
MH  - Animals
MH  - Apoptosis Regulatory Proteins/genetics/*immunology
MH  - Bone Marrow Cells/*metabolism/microbiology
MH  - Calcium-Binding Proteins/genetics/*immunology
MH  - Flagellin/genetics/immunology
MH  - Macrophages/*immunology/microbiology
MH  - Mice
MH  - Mice, Knockout
MH  - Mutation, Missense
MH  - NLR Family, Pyrin Domain-Containing 3 Protein/genetics/*immunology
MH  - Protein Domains
MH  - Salmonella Infections/genetics/*immunology
MH  - Salmonella typhimurium/genetics/*immunology
PMC - PMC4886354
EDAT- 2016/05/04 06:00
MHDA- 2017/07/22 06:00
PMCR- 2016/11/30
CRDT- 2016/05/04 06:00
PHST- 2013/10/24 00:00 [received]
PHST- 2016/04/12 00:00 [accepted]
PHST- 2016/05/04 06:00 [entrez]
PHST- 2016/05/04 06:00 [pubmed]
PHST- 2017/07/22 06:00 [medline]
PHST- 2016/11/30 00:00 [pmc-release]
AID - jem.20132234 [pii]
AID - 20132234 [pii]
AID - 10.1084/jem.20132234 [doi]
PST - ppublish
SO  - J Exp Med. 2016 May 30;213(6):877-85. doi: 10.1084/jem.20132234. Epub 2016 May 2.