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</radialGradient> </defs> <path style="fill:url(#MO_52ae16);stroke:none;" d="M 60 48.5415 c 0.8103 -7.397 2.3214 -19.8066 -3.5398 -20.1631 c 9.5776 -10.3066 -2.5463 -7.5712 3.5398 -16.9193 c -7.1467 -3.0187 -19.0893 -8.2203 -21.2568 -3.0292 c -7.3468 -11.8479 -8.3579 -0.0366 -15.8253 -8.4299 c -5.2269 5.5315 -14.1193 14.7258 -9.5978 18.2907 c -14.118 2.984 -2.6193 7.5483 -13.3201 11.7096 c 3.9166 6.4373 10.3631 17.3217 15.3246 14.3334 c -1.3787 13.6923 6.7392 4.7019 7.5932 15.6663 c 7.6473 -1.5531 20.5241 -4.0206 19.0691 -9.4324 c 13.2666 5.4782 6.7842 -4.643 18.013 -2.0267 z" /> </svg> PMID: 17379560, 12527755, 12514169 Nod2 senses both Gram-negative and Gram-positive bacteria since it recognizes MDP. PMID: 17379560, 12791997 Nod1, in contrast, has a narrow specificity and recognizes only diaminopimelic acid (DAP) type PG. PMID: 17379560 Very recently RIG-I and MDA-5 helicases have been shown to be intracellular sensors of viral double strand RNA. PMID: 17379560 Very recently RIG-I and MDA-5 helicases have been shown to be intracellular sensors of viral double strand RNA. PMID: 17379560, 10880512 Ligand recognition by the LRR domain of Nod1 or Nod2 is thought to induce a conformational change, allowing for the oligomerization of the molecule via the NACHT domain, and subsequent recruitment of the CARD domain adaptor RIP2 (RICK). PMID: 17379560, 10880512 Ligand recognition by the LRR domain of Nod1 or Nod2 is thought to induce a conformational change, allowing for the oligomerization of the molecule via the NACHT domain, and subsequent recruitment of the CARD domain adaptor RIP2 (RICK). PMID: 17379560, 10880512 Ligand recognition by the LRR domain of Nod1 or Nod2 is thought to induce a conformational change, allowing for the oligomerization of the molecule via the NACHT domain, and subsequent recruitment of the CARD domain adaptor RIP2 (RICK). PMID: 17379560, 10880512 Ligand recognition by the LRR domain of Nod1 or Nod2 is thought to induce a conformational change, allowing for the oligomerization of the molecule via the NACHT domain, and subsequent recruitment of the CARD domain adaptor RIP2 (RICK). PMID: 17379560, 11463746 Upon Nod1 activation, a transient interaction between Nod1, RIP2 and IKKs occurs, which is suggestive of a mechanism of down-regulation. indirect indirect PMID: 17379560, 15620648 Activation of Nod2 has been shown to induce a RIP2-dependent ubiquitinylation of NEMO (IKKγ), at a novel site, resulting in enhanced NF-κB signaling PMID: 17379560, 10329646 Nod1 has been shown to bind to pro-caspase 9, through homophilic CARD-CARD interactions and up-regulate caspase-9 induced apoptosis. indirect PMID: 17379560 pro-IL-1ß processing and IL-1ß secretion relies on cleavage of pro-IL-1ß by caspase-1. This process takes place in a protein complex recently described as the “inflammasome”. PMID: 17379560, 12191486 The “inflammasome” comprises of caspase-1 and -5, the adaptor protein ASC, which bears a CARD and a PYRIN domain, and several members from the Nalp family, which are NACHT proteins bearing both a PYRIN and a LRR domain. PMID: 17379560, 12459189 Nod1 enhances pro-interleukin-1ß processing through heterophilic CARD-CARD interactions between Nod1, RIP2 and pro-caspase-1. PMID: 17379560, 15530394 It has also been published that MDP can activate the inflammasome through binding to Nalp3 (cryopyrin). indirect PMID: 17379560, 15530394 It has also been published that MDP can activate the inflammasome through binding to Nalp3 (cryopyrin). PMID: 17379560, 15657077 TRIP-6, a LIM-domain containing protein, can potentiate Nod1 activation, most likely through its interaction with RIP2. PMID: 17379560, 15075345 TAK1 and Nod2 have been shown to interact through the LRR domain of Nod2 and to reciprocally negatively regulate NF-κB activation. PMID: 17379560, 15075345 TAK1 and Nod2 have been shown to interact through the LRR domain of Nod2 and to reciprocally negatively regulate NF-κB activation. PMID: 17379560, 16714539, 16203728 ERBIN appears to be a negative regulator of Nod2 dependent NF-κB and MAP kinases signaling PMID: 17379560, 15620648 More recently, activation of Nod2 has been shown to induce a RIP2-dependent ubiquitinylation of NEMO (IKKg), at a novel site, resulting in enhanced NFkB signaling PMID: 17379560 ERBIN, a member of the LAP (LRR and PDZ domain) protein family involved in cell polarity, as a new binding partner of Nod2.