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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.