Eunjoon Kim

TL;DR: 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.

TL;DR: 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.

TL;DR: 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.

TL;DR: 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.

TL;DR: In this article, an interaction between NMDA receptor subunits 2A and 2B (NR2A and NR2B) and three distinct members of the PSD-95/SAP90 family of membrane-associated putative guanylate kinases was identified.