Detection of PSD‑95 by Western Blot. Western blot of rat hippocampus lysate showing specific immunolabeling of the approximately 95 kDa PSD-95 protein.
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Stability & Storage
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PSD-95 (postsynaptic density-95 kDa; also SAP90) is a 95 kDa member of the MAGUK (membrane-associated guanylate kinase) family of molecules. It is a multidomain protein that serves as a scaffold, or anchor, for the organization of structural and signal transduction pathways in neurons. It is capable of forming multimers, generating large complexes that impact the size and strength of synapses. The molecule is highly conserved across species, being 99% amino acid identical, human to rodent. In rats, PSD-95 is 724 amino acids (aa) in length, and contains three consecutive 80 aa PDZ domains (aa 65 - 393), followed by an SH3 domain (aa 432-490) and a C-terminal guanylate kinase domain (aa 534-709). The PZD (PSD/Discs-large/ZO-1) domains in PSD-95 are globular structures that bind NMDA receptor subunits and neuroligin (a transmembrane intercellular neuron adhesion molecule). The SH3 domain binds proline-rich motifs on enzymes, and may interact with either kainate receptor subunits or SHANK, another scaffold protein. The guanylate kinase binds microtubules-associated protein and kainate receptor subunits. PSD-95 is regulated by palmitoylation on C3 and C5. When present, palmitate promotes AMPA receptor clustering and neurotransmission. Phosphorylation also regulates PSD-95 activity. Both S290 and S295 are known to be phosphorylated. These modifications are suggested to retain PSD-95 in the synapse and/or regulate PZD interactions with target proteins.
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Postsynaptic Density Protein 95/Disks Large Homolog 4
Entrez Gene IDs:
discs, large homolog 4 (Drosophila); disks large homolog 4; DLG4; FLJ97752; FLJ98574; Postsynaptic density protein 95; post-synaptic density protein 95; PSD95; PSD-95; PSD95SAP90SAP-90discs large homolog 4; SAP90; Synapse-associated protein 90; Tax interaction protein 15
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