Journal
SCIENCE
Volume 366, Issue 6464, Pages 460-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aau6391
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Funding
- Natural Science Foundation of China (NSFC) [31770938, 91854113]
- Key Program of Zhejiang Provincial Natural Science Foundation of China [LZ16C050001]
- NSFC [31771525, 91754113]
- Ministry of Science and Technology of the People's Republic of China [2017YFA0503402]
- Canadian Institutes of Health Research (CIHR) [MOP-133656, PJT-166010]
- J. P. Bickell Foundation
- CIHR (FDN) [154329]
- CIHR (FND) [143203]
- Leona M. and Harry B. Helmsley Charitable Trust
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The nucleotide oligomerization domain (NOD)-like receptors 1 and 2 (NOD1/2) are intracellular pattern-recognition proteins that activate immune signaling pathways in response to peptidoglycans associated with microorganisms. Recruitment to bacteria-containing endosomes and other intracellular membranes is required for NOD1/2 signaling, and NOD1/2 mutations that disrupt membrane localization are associated with inflammatory bowel disease and other inflammatory conditions. However, little is known about this recruitment process. We found that NOD1/2 S-palmitoylation is required for membrane recruitment and immune signaling. ZDHHC5 was identified as the palmitoyltransferase responsible for this critical posttranslational modification, and several disease-associated mutations in NOD2 were found to be associated with defective S-palmitoylation. Thus, ZDHHC5-mediated S-palmitoylation of NOD1/2 is critical for their ability to respond to peptidoglycans and to mount an effective immune response.
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