Functional architecture of the synaptic transducers at a central glutamatergic synapse

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Functional architecture of the synaptic transducers at a central glutamatergic synapse. / Brockmann, Marisa; Toulme, Estelle; Grasskamp, Andreas; Trimbuch, Thorsten; Südhof, Thomas; Walter, Alexander; Rosenmund, Christian.

2020.

Research output: Working paper › Preprint › Research

Harvard

Brockmann, M, Toulme, E, Grasskamp, A, Trimbuch, T, Südhof, T, Walter, A & Rosenmund, C 2020 'Functional architecture of the synaptic transducers at a central glutamatergic synapse'. https://doi.org/10.1101/2020.12.25.424391

APA

Brockmann, M., Toulme, E., Grasskamp, A., Trimbuch, T., Südhof, T., Walter, A., & Rosenmund, C. (2020). Functional architecture of the synaptic transducers at a central glutamatergic synapse. https://doi.org/10.1101/2020.12.25.424391

Vancouver

Brockmann M, Toulme E, Grasskamp A, Trimbuch T, Südhof T, Walter A et al. Functional architecture of the synaptic transducers at a central glutamatergic synapse. 2020. https://doi.org/10.1101/2020.12.25.424391

Author

Brockmann, Marisa ; Toulme, Estelle ; Grasskamp, Andreas ; Trimbuch, Thorsten ; Südhof, Thomas ; Walter, Alexander ; Rosenmund, Christian. / Functional architecture of the synaptic transducers at a central glutamatergic synapse. 2020.

Bibtex

@techreport{99c3ef0ca50a464abdc7c13e5382ce9e,
title = "Functional architecture of the synaptic transducers at a central glutamatergic synapse",
abstract = "Neuronal synapses transduce information via the consecutive action of three transducers: voltage-gated Ca2+-channels, fusion-competent synaptic vesicles, and postsynaptic receptors. Their physical distance is thought to influence the speed and efficiency of neurotransmission. However, technical limitations have hampered resolving their nanoscale arrangement. Here, we developed a new method for live-labeling proteins for electron microscopy (EM), revealing that release-competent vesicles preferentially align with Ca2+-channels and postsynaptic AMPA receptors within 20-30 nm and thereby forming a transsynaptic tripartite nanocomplex. Using functional EM, we show that single action potentials cause vesicles within the nanocomplex to fuse with a 50% probability. The loss of the presynaptic scaffold disrupts the formation of the tripartite transducers. Strikingly, the forced transsynaptic alignment of the Ca2+-channel subunit α2δ1 and AMPA receptors suffice to restore neurotransmission in a scaffold lacking synapse. Our results demonstrate a synaptic transducer nanocomplex that actively contributes to the organization of central synapses",
author = "Marisa Brockmann and Estelle Toulme and Andreas Grasskamp and Thorsten Trimbuch and Thomas S{\"u}dhof and Alexander Walter and Christian Rosenmund",
year = "2020",
doi = "10.1101/2020.12.25.424391",
language = "English",
type = "WorkingPaper",

}

RIS

TY - UNPB

T1 - Functional architecture of the synaptic transducers at a central glutamatergic synapse

AU - Brockmann, Marisa

AU - Toulme, Estelle

AU - Grasskamp, Andreas

AU - Trimbuch, Thorsten

AU - Südhof, Thomas

AU - Walter, Alexander

AU - Rosenmund, Christian

PY - 2020

Y1 - 2020

N2 - Neuronal synapses transduce information via the consecutive action of three transducers: voltage-gated Ca2+-channels, fusion-competent synaptic vesicles, and postsynaptic receptors. Their physical distance is thought to influence the speed and efficiency of neurotransmission. However, technical limitations have hampered resolving their nanoscale arrangement. Here, we developed a new method for live-labeling proteins for electron microscopy (EM), revealing that release-competent vesicles preferentially align with Ca2+-channels and postsynaptic AMPA receptors within 20-30 nm and thereby forming a transsynaptic tripartite nanocomplex. Using functional EM, we show that single action potentials cause vesicles within the nanocomplex to fuse with a 50% probability. The loss of the presynaptic scaffold disrupts the formation of the tripartite transducers. Strikingly, the forced transsynaptic alignment of the Ca2+-channel subunit α2δ1 and AMPA receptors suffice to restore neurotransmission in a scaffold lacking synapse. Our results demonstrate a synaptic transducer nanocomplex that actively contributes to the organization of central synapses

AB - Neuronal synapses transduce information via the consecutive action of three transducers: voltage-gated Ca2+-channels, fusion-competent synaptic vesicles, and postsynaptic receptors. Their physical distance is thought to influence the speed and efficiency of neurotransmission. However, technical limitations have hampered resolving their nanoscale arrangement. Here, we developed a new method for live-labeling proteins for electron microscopy (EM), revealing that release-competent vesicles preferentially align with Ca2+-channels and postsynaptic AMPA receptors within 20-30 nm and thereby forming a transsynaptic tripartite nanocomplex. Using functional EM, we show that single action potentials cause vesicles within the nanocomplex to fuse with a 50% probability. The loss of the presynaptic scaffold disrupts the formation of the tripartite transducers. Strikingly, the forced transsynaptic alignment of the Ca2+-channel subunit α2δ1 and AMPA receptors suffice to restore neurotransmission in a scaffold lacking synapse. Our results demonstrate a synaptic transducer nanocomplex that actively contributes to the organization of central synapses

U2 - 10.1101/2020.12.25.424391

DO - 10.1101/2020.12.25.424391

M3 - Preprint

BT - Functional architecture of the synaptic transducers at a central glutamatergic synapse

ER -

ID: 334078983