GluR2Q and GluR2R AMPA Subunits are not Targets of lypd2 Interaction

A large family of prototoxin-like molecules endogenous to mammals, Ly6 proteins have been implicated in the regulation of cell signaling processes across multiple species. Previous work has shown that certain members of the Ly6 family are expressed in the brain and target nicotinic acetylcholine receptor and potassium channel function. Structural similarities between Ly6 proteins and alpha-neurotoxins suggest the possibility of additional ionotropic receptor targets. Here, we investigated the possibility of lypd2 as a novel regulator of AMPA receptor (AMPAR) function. In particular, we focused on potential interactions with the Q/R isoforms of the GluR2 subunit, which have profound impacts on AMPAR permeability to calcium during neuronal stimulation. We find that although lypd2 and GluR2 share overlapping expression patterns in the mouse hippocampus, there was no interaction between lypd2 and either GluR2(Q) or GluR2(R) isoform. These results underscore the importance of continuing to investigate novel targets for Ly6 interaction and regulation.

Automated summary

Ly6 proteins, a large family of prototoxin-like molecules endogenous to mammals, have been implicated in regulating cell signaling processes. This study investigated the possibility of lypd2 as a regulator of AMPAR function and found that there was no interaction between lypd2 and specific isoforms of GluR2, highlighting the importance of further investigating novel targets for Ly6 interaction and regulation.