The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones

Research output: Contribution to journal › Journal article › Research › peer-review

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The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones. / Imig, Cordelia; Min, Sang-Won; Krinner, Stefanie; Arancillo, Marife; Rosenmund, Christian; Südhof, Thomas C; Rhee, JeongSeop; Brose, Nils; Cooper, Benjamin H.

In: Neuron, Vol. 84, No. 2, 22.10.2014, p. 416-31.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Imig, C, Min, S-W, Krinner, S, Arancillo, M, Rosenmund, C, Südhof, TC, Rhee, J, Brose, N & Cooper, BH 2014, 'The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones', Neuron, vol. 84, no. 2, pp. 416-31. https://doi.org/10.1016/j.neuron.2014.10.009

APA

Imig, C., Min, S-W., Krinner, S., Arancillo, M., Rosenmund, C., Südhof, T. C., Rhee, J., Brose, N., & Cooper, B. H. (2014). The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones. Neuron, 84(2), 416-31. https://doi.org/10.1016/j.neuron.2014.10.009

Vancouver

Imig C, Min S-W, Krinner S, Arancillo M, Rosenmund C, Südhof TC et al. The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones. Neuron. 2014 Oct 22;84(2):416-31. https://doi.org/10.1016/j.neuron.2014.10.009

Author

Imig, Cordelia ; Min, Sang-Won ; Krinner, Stefanie ; Arancillo, Marife ; Rosenmund, Christian ; Südhof, Thomas C ; Rhee, JeongSeop ; Brose, Nils ; Cooper, Benjamin H. / The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones. In: Neuron. 2014 ; Vol. 84, No. 2. pp. 416-31.

Bibtex

@article{c476a95109834429a8bd00942abfe6a8,
title = "The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones",
abstract = "Synaptic vesicle docking, priming, and fusion at active zones are orchestrated by a complex molecular machinery. We employed hippocampal organotypic slice cultures from mice lacking key presynaptic proteins, cryofixation, and three-dimensional electron tomography to study the mechanism of synaptic vesicle docking in the same experimental setting, with high precision, and in a near-native state. We dissected previously indistinguishable, sequential steps in synaptic vesicle active zone recruitment (tethering) and membrane attachment (docking) and found that vesicle docking requires Munc13/CAPS family priming proteins and all three neuronal SNAREs, but not Synaptotagmin-1 or Complexins. Our data indicate that membrane-attached vesicles comprise the readily releasable pool of fusion-competent vesicles and that synaptic vesicle docking, priming, and trans-SNARE complex assembly are the respective morphological, functional, and molecular manifestations of the same process, which operates downstream of vesicle tethering by active zone components. ",
keywords = "Animals, Hippocampus/metabolism, Membrane Fusion/physiology, Mice, Neurons/metabolism, SNARE Proteins/metabolism, Synapses/metabolism, Synaptic Transmission/physiology, Synaptic Vesicles/metabolism",
author = "Cordelia Imig and Sang-Won Min and Stefanie Krinner and Marife Arancillo and Christian Rosenmund and S{\"u}dhof, {Thomas C} and JeongSeop Rhee and Nils Brose and Cooper, {Benjamin H}",
year = "2014",
month = oct,
day = "22",
doi = "10.1016/j.neuron.2014.10.009",
language = "English",
volume = "84",
pages = "416--31",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "2",

}

RIS

TY - JOUR

T1 - The morphological and molecular nature of synaptic vesicle priming at presynaptic active zones

AU - Imig, Cordelia

AU - Min, Sang-Won

AU - Krinner, Stefanie

AU - Arancillo, Marife

AU - Rosenmund, Christian

AU - Südhof, Thomas C

AU - Rhee, JeongSeop

AU - Brose, Nils

AU - Cooper, Benjamin H

PY - 2014/10/22

Y1 - 2014/10/22

N2 - Synaptic vesicle docking, priming, and fusion at active zones are orchestrated by a complex molecular machinery. We employed hippocampal organotypic slice cultures from mice lacking key presynaptic proteins, cryofixation, and three-dimensional electron tomography to study the mechanism of synaptic vesicle docking in the same experimental setting, with high precision, and in a near-native state. We dissected previously indistinguishable, sequential steps in synaptic vesicle active zone recruitment (tethering) and membrane attachment (docking) and found that vesicle docking requires Munc13/CAPS family priming proteins and all three neuronal SNAREs, but not Synaptotagmin-1 or Complexins. Our data indicate that membrane-attached vesicles comprise the readily releasable pool of fusion-competent vesicles and that synaptic vesicle docking, priming, and trans-SNARE complex assembly are the respective morphological, functional, and molecular manifestations of the same process, which operates downstream of vesicle tethering by active zone components.

AB - Synaptic vesicle docking, priming, and fusion at active zones are orchestrated by a complex molecular machinery. We employed hippocampal organotypic slice cultures from mice lacking key presynaptic proteins, cryofixation, and three-dimensional electron tomography to study the mechanism of synaptic vesicle docking in the same experimental setting, with high precision, and in a near-native state. We dissected previously indistinguishable, sequential steps in synaptic vesicle active zone recruitment (tethering) and membrane attachment (docking) and found that vesicle docking requires Munc13/CAPS family priming proteins and all three neuronal SNAREs, but not Synaptotagmin-1 or Complexins. Our data indicate that membrane-attached vesicles comprise the readily releasable pool of fusion-competent vesicles and that synaptic vesicle docking, priming, and trans-SNARE complex assembly are the respective morphological, functional, and molecular manifestations of the same process, which operates downstream of vesicle tethering by active zone components.

KW - Animals

KW - Hippocampus/metabolism

KW - Membrane Fusion/physiology

KW - Mice

KW - Neurons/metabolism

KW - SNARE Proteins/metabolism

KW - Synapses/metabolism

KW - Synaptic Transmission/physiology

KW - Synaptic Vesicles/metabolism

U2 - 10.1016/j.neuron.2014.10.009

DO - 10.1016/j.neuron.2014.10.009

M3 - Journal article

C2 - 25374362

VL - 84

SP - 416

EP - 431

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 2

ER -

ID: 237698103