The presynaptic particle web: ultrastructure, composition, dissolution, and reconstitution
| Autor: | G R, Phillips, J K, Huang, Y, Wang, H, Tanaka, L, Shapiro, W, Zhang, W S, Shan, K, Arndt, M, Frank, R E, Gordon, M A, Gawinowicz, Y, Zhao, D R, Colman |
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| Rok vydání: | 2001 |
| Předmět: |
Dynamins
Male Myosin Heavy Chains Synaptosomal-Associated Protein 25 Qa-SNARE Proteins Cell Membrane Presynaptic Terminals Vesicular Transport Proteins Membrane Proteins Spectrin Nerve Tissue Proteins Cadherins Synapsins Antibodies Clathrin GTP Phosphohydrolases Rats Munc18 Proteins Neurofilament Proteins Clathrin Heavy Chains Animals HSP70 Heat-Shock Proteins Rabbits Synaptic Vesicles Microscopy Immunoelectron |
| Zdroj: | Neuron. 32(1) |
| ISSN: | 0896-6273 |
| Popis: | We report the purification of a presynaptic "particle web" consisting of approximately 50 nm pyramidally shaped particles interconnected by approximately 100 nm spaced fibrils. This is the "presynaptic grid" described in early EM studies. It is completely soluble above pH 8, but reconstitutes after dialysis against pH 6. Interestingly, reconstituted particles orient and bind PSDs asymmetrically. Mass spectrometry of purified web components reveals major proteins involved in the exocytosis of synaptic vesicles and in membrane retrieval. Our data support the idea that the CNS synaptic junction is organized by transmembrane adhesion molecules interlinked in the synaptic cleft, connected via their intracytoplasmic domains to the presynaptic web on one side and to the postsynaptic density on the other. The CNS synaptic junction may therefore be conceptualized as a complicated macromolecular scaffold that isostatically bridges two closely aligned plasma membranes. |
| Databáze: | OpenAIRE |
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