2013年5月20日 · Here, we review the effects of subunit composition on NMDAR properties, synaptic plasticity and cellular mechanisms implicated in neuropsychiatric disorders. Understanding the rules and roles of...

We show that glycine-independent desensitization is controlled by N-terminal domains of the NR2 subunit that flank the putative agonist-binding domain: a four amino acid (aa) segment immediately preceding the first transmembrane domain (M1) and a region containing the leucine/isoleucine/valine–binding protein–like (LIVBP-like) domain.

In mature cultured neurons, NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expres-sion of GluR1, primarily by regulating its surface in-sertion. In mature neurons, NR2B is coupled to inhibi-tion rather than activation of the Ras-ERK pathway, which drives surface delivery of GluR1.

2008年8月1日 · Fukaya et al. 63 showed that NR1 was vital for the release of NR2 subunits from the ER in hippocampal pyramidal cells in vivo: in the absence of NR1, the NR2 subunits are retained and aggregated into intracisternal granules.

2001年11月1日 · Here we show that the NR2 receptor is recognized by both murine and human anti-DNA antibodies. Moreover, anti-DNA antibodies with this cross-reactivity mediate apoptotic death of neurons in vivo...

2003年1月1日 · NMDA receptors are composed of seven known subunits (NR1, NR2A–D, NR3A–B). The present review focuses on the NR2B subunit of the receptor. Over the last several years, an increasing number of reports have demonstrated the importance of the NR2B subunit in a variety of synaptic signaling events and protein-protein interactions.

2007年9月30日 · We evaluated the potency and efficacy of a wide range of glutamate-like compounds at NR1/NR2A, NR1/NR2B, NR1/NR2C, and NR1/NR2D receptors. Twenty-five of 53 compounds examined exhibited agonist activity at the glutamate binding site of NMDA receptors. Concentration-response relationships were determined for these agonists at each NR2 subunit.

2025年2月25日 · Huang et al. present the cryo-EM structures of human GluN1-N2B receptors in the Mg2+ bound and Mg2+ free states and identify three Mg2+-binding sites with distinct regulatory functions: site Ⅰ for the voltage-dependent block, site Ⅱ for the GluN2B-specific potentiation, and site Ⅲ for the NTD-driven allosteric inhibition.

The incorporation of different NR2 subunits has a major impact on the functional properties of the NMDA receptor, critically influencing agonist and antagonist affinity, receptor deactivation kinetics, channel conductance and interactions with intracellular proteins .

2007年4月22日 · Four different NR2 subunits (NR2A-D) have been identified with distinct expression and functional profiles (Erreger et al., 2004). This heterogeneity among NMDA receptor subunits creates an opportunity to identify subunit selective agonists, partial agonists, antagonists, and modulators.