Cypin: a cytosolic regulator of PSD-95 postsynaptic targeting
| Autor: | B L, Firestein, J E, Brenman, C, Aoki, A M, Sanchez-Perez, A E, El-Husseini, D S, Bredt |
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| Rok vydání: | 1999 |
| Předmět: |
Cerebral Cortex
Guanine Deaminase Neurons Binding Sites Molecular Sequence Data Intracellular Signaling Peptides and Proteins Presynaptic Terminals Brain Membrane Proteins Nerve Tissue Proteins Intracellular Membranes Chemical Fractionation Rats Cytosol Synapses Animals Amino Acid Sequence Intestinal Mucosa Carrier Proteins Nucleoside-Phosphate Kinase Disks Large Homolog 4 Protein Guanylate Kinases |
| Zdroj: | Neuron. 24(3) |
| ISSN: | 0896-6273 |
| Popis: | Postsynaptic density 95 (PSD-95/SAP-90) is a membrane associated guanylate kinase (GK) PDZ protein that scaffolds glutamate receptors and associated signaling networks at excitatory synapses. Affinity chromatography identifies cypin as a major PSD-95-binding protein in brain extracts. Cypin is homologous to a family of hydrolytic bacterial enzymes and shares some similarity with collapsin response mediator protein (CRMP), a cytoplasmic mediator of semaphorin III signalling. Cypin is discretely expressed in neurons and is polarized to basal membranes in intestinal epithelial cells. Overexpression of cypin in hippocampal neurons specifically perturbs postsynaptic trafficking of PSD-95 and SAP-102, an effect not produced by overexpression of other PDZ ligands. In fact, PSD-95 can induce postsynaptic clustering of an otherwise diffusely localized K+ channel, Kv1.4. By regulating postsynaptic protein sorting, cypin may influence synaptic development and plasticity. |
| Databáze: | OpenAIRE |
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