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- Title
Evaluation of Nod-Like Receptor (NLR) Effector Domain Interactions.
- Authors
Wagner, Roland N.; Proell, Martina; Kufer, Thomas A.; Schwarzenbacher, Robert
- Abstract
Members of the Nod-like receptor (NLR) family recognize intracellular pathogens and recruit a variety of effector molecules, including pro-caspases and kinases, which in turn are implicated in cytokine processing and NF-kB activation. In order to elucidate the intricate network of NLR signaling, which is still fragmentary in molecular terms, we applied comprehensive yeast two-hybrid analysis for unbiased evaluation of physical interactions between NLRs and their adaptors (ASC, CARD8) as well as kinase RIPK2 and inflammatory caspases (C1, C2, C4, C5) under identical conditions. Our results confirmed the interaction of NOD1 and NOD2 with RIPK2, and between NLRP3 and ASC, but most importantly, our studies revealed hitherto unrecognized interactions of NOD2 with members of the NLRP subfamily. We found that NOD2 specifically and directly interacts with NLRP1, NLRP3 and NLRP12. Furthermore, we observed homodimerization of the RIPK2 CARD domains and identified residues in NOD2 critical for interaction with RIPK2. In conclusion, our work provides further evidence for the complex network of protein-protein interactions underlying NLR function.
- Subjects
PROTEIN-protein interactions; INTRACELLULAR pathogens; PATHOGENIC microorganisms; MOLECULES; CELL receptors; MEDICAL microbiology; CHEMICAL templates; CYTOKINES; CELLULAR immunity; BINDING sites
- Publication
PLoS ONE, 2009, Vol 4, Issue 4, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0004931