RGD Reference Report - A trans-synaptic nanocolumn aligns neurotransmitter release to receptors. - Rat Genome Database

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A trans-synaptic nanocolumn aligns neurotransmitter release to receptors.

Authors: Tang, Ai-Hui  Chen, Haiwen  Li, Tuo P  Metzbower, Sarah R  MacGillavry, Harold D  Blanpied, Thomas A 
Citation: Tang AH, etal., Nature. 2016 Aug 11;536(7615):210-4. doi: 10.1038/nature19058. Epub 2016 Jul 27.
RGD ID: 13702367
Pubmed: PMID:27462810   (View Abstract at PubMed)
PMCID: PMC5002394   (View Article at PubMed Central)
DOI: DOI:10.1038/nature19058   (Journal Full-text)

Synaptic transmission is maintained by a delicate, sub-synaptic molecular architecture, and even mild alterations in synapse structure drive functional changes during experience-dependent plasticity and pathological disorders. Key to this architecture is how the distribution of presynaptic vesicle fusion sites corresponds to the position of receptors in the postsynaptic density. However, while it has long been recognized that this spatial relationship modulates synaptic strength, it has not been precisely described, owing in part to the limited resolution of light microscopy. Using localization microscopy, here we show that key proteins mediating vesicle priming and fusion are mutually co-enriched within nanometre-scale subregions of the presynaptic active zone. Through development of a new method to map vesicle fusion positions within single synapses in cultured rat hippocampal neurons, we find that action-potential-evoked fusion is guided by this protein gradient and occurs preferentially in confined areas with higher local density of Rab3-interacting molecule (RIM) within the active zones. These presynaptic RIM nanoclusters closely align with concentrated postsynaptic receptors and scaffolding proteins, suggesting the existence of a trans-synaptic molecular 'nanocolumn'. Thus, we propose that the nanoarchitecture of the active zone directs action-potential-evoked vesicle fusion to occur preferentially at sites directly opposing postsynaptic receptor-scaffold ensembles. Remarkably, NMDA receptor activation triggered distinct phases of plasticity in which postsynaptic reorganization was followed by trans-synaptic nanoscale realignment. This architecture suggests a simple organizational principle of central nervous system synapses to maintain and modulate synaptic efficiency.




Cellular Component

  
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Original Reference(s)
Rims1Ratglutamatergic synapse is_active_inIDA PMID:27462810SynGO 
Rims1Ratpresynaptic active zone cytoplasmic component is_active_inIDA PMID:27462810SynGO 


Genes (Rattus norvegicus)
Rims1  (regulating synaptic membrane exocytosis 1)