Activity-Dependent Internalization of Glun2B-Containing NMDARS Is Required For Synaptic Incorporation of Glun2A And Synaptic Plasticity.

NMDA-type glutamate receptors are heterotetrameric complexes composed of two GluN1 and two GluN2 subunits. The precise composition of the GluN2 subunits determines the channel's biophysical properties and influences its interaction with postsynaptic scaffolding proteins and signaling molecules involved in synaptic physiology and plasticity. The precise regulation of NMDAR subunit composition at synapses is crucial for proper synaptogenesis, neuronal circuit development, and synaptic plasticity, a cellular model of memory formation.

[Percutaneous Resolution for Tricuspid Stenosis: Positive Outcomes Despite High Surgical Risk].

We report a 31-year-old woman who was previously subjected to aortic, mitral, and tricuspid valve replacement in three different surgical episodes. She was admitted to our cardiology section with acute right heart failure symptoms. She was studied by echocardiography, right/left heart catheterization, cardiac CT scan and cardiac magnetic resonance.

Early expression of GluN2A-containing NMDA receptors in a model of fragile X syndrome.

NMDA-type glutamate receptors (NMDARs) play a crucial role in synaptogenesis, circuit development, and synaptic plasticity, serving as fundamental components in cellular models of learning and memory. Their dysregulation has been implicated in several neurological disorders and synaptopathies. NMDARs are heterotetrameric complexes composed of two GluN1 and two GluN2 subunits.

ROR2 homodimerization is sufficient to activate a neuronal Wnt/calcium signaling pathway.

Wnt signaling plays a key role in the mature CNS by regulating trafficking of NMDA-type glutamate receptors and intrinsic properties of neurons. The Wnt receptor ROR2 has been identified as a necessary component of the neuronal Wnt5a/Ca signaling pathway that regulates synaptic and neuronal function. Since ROR2 is considered a pseudokinase, its mechanism for downstream signaling upon ligand binding has been controversial.