NOD-like receptor signaling pathway

Specific families of pattern recognition receptors play a key role in recognizing various pathogens and generating innate immune responses. Nucleotide-binding, oligomerization domain (NOD)-like receptors (NLRs) are a family of cytosolic proteins that play a pivotal role in the recognition of intracellular ligands. The NLR family contains twenty-two human proteins and at least thirty-four mouse proteins that include a central nucleotide-binding, oligomerization domain (NOD or NACHT), an N-terminal protein interaction domain, and a variable number of C-terminal leucine-rich repeats. Similar to the leucine-rich repeat-containing toll-like receptors (TLRs), multiple NLRs function as pattern recognition receptors. These NLRs are responsible for detecting specific pathogen-associated molecules or host-derived damage signals in the cytosol and initiating the innate immune response. NOD1 and NOD2, two prototypic NLRs, are activated by specific components of bacterial peptidoglycan that escaped from endosomal compartments. Their activation triggers several signaling pathways, including the activation of NF-κB and MAPK, cytokine production and apoptosis. Additionally, activation of NOD1 and NOD2 can induce autophagy through an interaction with Autophagy-related 16-like 1 (ATG16L1). On the other hand, a different set of NLRs induces caspase-1 activation through the assembly of multiprotein complexes called inflammasomes. The activated of caspase-1 regulates maturation of the pro-inflammatory cytokines IL-1B, IL-18 and drives pyroptosis. Although a clear connection between NOD1 and chronic inflammatory diseases has not been well-established, mutations in NOD2 have been linked to Crohn's disease and Blau syndrome.


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