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Role of NMDA Receptor Subtypes in Governing the Direction of Hippocampal Synaptic Plasticity
Using hippocampal slice preparations, it is shown that selectively blocking NMDARs that contain the NR2B subunit abolishes the induction of LTD but not LTP, demonstrating that distinct N MDAR subunits are critical factors that determine the polarity of synaptic plasticity. Expand
PDZ domain proteins of synapses
PDZ domains are protein-interaction domains that are often found in multi-domain scaffolding proteins that function in the dynamic trafficking of synaptic proteins by assembling cargo complexes for transport by molecular motors. Expand
Coupling of mGluR/Homer and PSD-95 Complexes by the Shank Family of Postsynaptic Density Proteins
It is reported that Shank proteins also bind to Homer, and Shank may cross-link Homer and PSD-95 complexes in the PSD and play a role in the signaling mechanisms of both mGluRs and NMDA receptors. Expand
Shank, a Novel Family of Postsynaptic Density Proteins that Binds to the NMDA Receptor/PSD-95/GKAP Complex and Cortactin
A novel family of postsynaptic density proteins, termed Shank, that binds via its PDZ domain to the C terminus of PSD-95-associated protein GKAP, and may function as a scaffold protein in the PSD, potentially cross-linking NMDA receptor/PSD- 95 complexes and coupling them to regulators of the actin cytoskeleton. Expand
Crystal Structures of a Complexed and Peptide-Free Membrane Protein–Binding Domain: Molecular Basis of Peptide Recognition by PDZ
X-ray crystallographic structures of the third PDZ domain from the synaptic protein PSD-95 in complex with and in the absence of its peptide ligand have been determined and reveal that specific side chain interactions and a prominent hydrophobic pocket explain the selective recognition of the C-terminal consensus sequence. Expand
Changing subunit composition of heteromeric NMDA receptors during development of rat cortex
Direct evidence is presented that NMDA receptors exist in rat neocortex as heteromeric complexes of considerable heterogeneity, some containing both NR2A and NR2B subunits. Expand
PDZ domains and the organization of supramolecular complexes.
PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ bindingExpand
The postsynaptic architecture of excitatory synapses: a more quantitative view.
The structures of some intact PSD proteins, as well as the spatial arrangement of several proteins within the PSD, have been determined at low resolution by electron microscopy, and a more quantitative and geometrically realistic view of PSD architecture is emerging. Expand
The Importance of Dendritic Mitochondria in the Morphogenesis and Plasticity of Spines and Synapses
The proper intracellular distribution of mitochondria is assumed to be critical for normal physiology of neuronal cells, and increasing dendritic mitochondrial content or mitochondrial activity enhances the number and plasticity of spines and synapses. Expand
Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
Functional and biochemical evidence is presented that cell-surface clustering of Shaker-subfamily K+ channels is mediated by the PSD-95 family of membrane-associated putative guanylate kinases, and the ability of PDZ domains to function as independent modules for protein–protein interaction, and their presence in other junction-associated molecules suggest that PDZ-domain-containing polypeptides may be widely involved in the organization of proteins at sites of membrane specialization. Expand