Kinetically distinct contributions of NMDA receptor NR1 and NR2 subunits to channel gating have recently been inferred by Banke and Traynelis from single-channel recordings of recombinant NR1–NR2B receptors. The results suggest a new mechanism for receptor activation that will enhance our insight into excitatory synaptic transmission in the brain. In the post-genomic era, this represents an exc...

We investigated the reactivity of several quinone methides (QMs) as activatable bis-alkylating agents capable of DNA cross-linking (XL-DNA) with promising potency. Taking advantage from a photochemical activation protocol of BINOL-derivatives, we had developed a new method for the resolution of 3,3’-CH2Xdisubstituted BINOL (X = NR2, SR, OH) studying as well the effect of electron-donating and e...

Modification of NMDA receptor function and trafficking contributes to the regulation of synaptic transmission and is important for several forms of synaptic plasticity. Here, we report that NMDA receptor subunits NR2A and NR2B have two distinct clusters of palmitoylation sites in their C-terminal region. Palmitoylation within the first cluster on a membrane-proximal region increases tyrosine ph...

Cellular-specific splicing of the retinal NMDAR1 receptor (NR1) and expression of NMDAR2 receptor (NR2) subunits in response to optic nerve injury was investigated by in situ hybridization in adult rats. A controlled optic nerve crush led to a clear alteration in the expression of alternatively spliced NR1 variants in the retinal ganglion cell layer (GCL). The NR1-2b and NR1-4b isoforms were pr...

BACKGROUND Ionotropic glutamate receptors in the central nervous system play a major role in numerous brain functions including learning and memory in many vertebrate species. NR2 subunits have been regarded as rate-limiting molecules in controlling the optimal N-methyl-D-aspartate (NMDA) receptor's coincidence-detection property and subsequent learning and memory function across multi-species....

We have identified a novel family of synaptic adhesion-like molecules (SALMs). The family members, SALM1-SALM4, have a single transmembrane (TM) domain and contain extracellular leucine-rich repeats, an Ig C2 type domain, a fibronectin type III domain, and an intracellular postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1 (PDZ) binding domain, which is present on all members except ...