Disease relevance of CPN2

• 2. There is a CPN2 soma and neuropilar arborization in each commissural ganglion (CoG) [1].

High impact information on CPN2

• In tetrameric CPN, each CPN1 subunit might interact with the central leucine-rich repeat tandem of the cognate CPN2 subunit via a unique hydrophobic surface patch wrapping around the catalytic domain-TT interface, exposing the two active centers [2].
• CPN2 also indirectly inhibits gastric mill neurons Int1 and VD (interneuron 1 and ventricular dilator neuron, respectively) through its activation of LG [1].
• The CPN2 excitatory effects are mediated at least partly via discrete excitatory postsynaptic potentials (EPSPs; Fig. 4B), whereas its inhibitory effects are produced via smooth hyperpolarizations [1].
• We also demonstrate that MPN has no proctolin-mediated influence on MCN1 or CPN2, although exogenously applied proctolin directly excites these neurons [3].

Chemical compound and disease context of CPN2

• Here, we show that MPN uses only its small molecule transmitter, GABA, to inhibit MCN1 and CPN2 within their ganglion of origin [3].

Anatomical context of CPN2

• Normally, CPN circulates in blood plasma as a hetero-tetramer consisting of two 83 kDa (CPN2) domains each flanked by a 48 to 55 kDa catalytic (CPN1) domain [2].

References