A Preformed Complex of Postsynaptic Proteins Is Involved in Excitatory Synapse Development
| Autor: | Kimberly Gerrow, Stefano Romorini, Carlo Sala, Michael A. Colicos, Alaa El-Husseini, Shahin M. Nabi |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Diagnostic Imaging
Scaffold protein Time Factors PROTEINS Cell Adhesion Molecules Neuronal Neuroscience(all) Green Fluorescent Proteins Models Neurological Presynaptic Terminals Synaptogenesis Nerve Tissue Proteins Pyridinium Compounds Biology Hippocampus MOLNEURO 03 medical and health sciences 0302 clinical medicine Excitatory synapse Postsynaptic potential Vesicular Glutamate Transport Proteins Phosphoprotein Phosphatases Animals RNA Small Interfering Rats Wistar Cells Cultured 030304 developmental biology Neurons 0303 health sciences Nocodazole General Neuroscience Intracellular Signaling Peptides and Proteins Membrane Proteins Embryo Mammalian Immunohistochemistry Actins Rats Cell biology Quaternary Ammonium Compounds Protein Transport Disks Large Homolog 4 Protein Synapses Excitatory postsynaptic potential Axoplasmic transport Dual-Specificity Phosphatases CELLBIO Postsynaptic density 030217 neurology & neurosurgery |
| Zdroj: | Neuron. 49(4):547-562 |
| ISSN: | 0896-6273 |
| DOI: | 10.1016/j.neuron.2006.01.015 |
| Popis: | SummaryNonsynaptic clusters of postsynaptic proteins have been documented; however, their role remains elusive. We monitored the trafficking of several candidate proteins implicated in synaptogenesis, when nonsynaptic clusters of scaffold proteins are most abundant. We find a protein complex consisting of two populations that differ in their content, mobility, and involvement in synapse formation. One subpopulation is mobile and relies on actin transport for delivery to nascent and existing synapses. These mobile clusters contain the scaffolding proteins PSD-95, GKAP, and Shank. A proportion of mobile clusters that exhibits slow movement and travels short distances contains neuroligin-1. The second group consists of stationary nonsynaptic scaffold complexes that mainly contain neuroligin-1, can recruit synaptophysin-containing axonal transport vesicles, and are readily transformed to functional presynaptic contacts that recycle the vital dye FM 4-64. These results postulate a mechanism whereby preformed scaffold protein complexes serve as predetermined postsynaptic hotspots for establishment of new functional excitatory synapses. |
| Databáze: | OpenAIRE |
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