Synapsin-dependent development of glutamatergic synaptic vesicles and presynaptic plasticity in postnatal mouse brain

Neuroscience ◽  
2009 ◽  
Vol 158 (1) ◽  
pp. 231-241 ◽  
Author(s):  
I.L. Bogen ◽  
V. Jensen ◽  
O. Hvalby ◽  
S.I. Walaas
Keyword(s):  
Mouse Brain ◽  
Synaptic Vesicles ◽  
Dependent Development ◽  
Presynaptic Plasticity

scholarly journals Author response: Frequency-dependent mobilization of heterogeneous pools of synaptic vesicles shapes presynaptic plasticity

2017 ◽  
Author(s):  
Frédéric Doussau ◽  
Hartmut Schmidt ◽  
Kevin Dorgans ◽  
Antoine M Valera ◽  
Bernard Poulain ◽  
...  
Keyword(s):  
Synaptic Vesicles ◽  
Author Response ◽  
Response Frequency ◽  
Frequency Dependent ◽  
Presynaptic Plasticity

scholarly journals Presynaptic Calcium Channels

2019 ◽  
Vol 20 (9) ◽  
pp. 2217 ◽  
Author(s):  
Sumiko Mochida
Keyword(s):  
Neurotransmitter Release ◽  
Synaptic Vesicles ◽  
Neuronal Firing ◽  
Regulatory Proteins ◽  
Channel Modulation ◽  
Signaling Complex ◽  
Presynaptic Plasticity ◽  
Presynaptic Calcium ◽  
Ca2 Channels ◽  
Α1 Subunit

Presynaptic Ca2+ entry occurs through voltage-gated Ca2+ (CaV) channels which are activated by membrane depolarization. Depolarization accompanies neuronal firing and elevation of Ca2+ triggers neurotransmitter release from synaptic vesicles. For synchronization of efficient neurotransmitter release, synaptic vesicles are targeted by presynaptic Ca2+ channels forming a large signaling complex in the active zone. The presynaptic CaV2 channel gene family (comprising CaV2.1, CaV2.2, and CaV2.3 isoforms) encode the pore-forming α1 subunit. The cytoplasmic regions are responsible for channel modulation by interacting with regulatory proteins. This article overviews modulation of the activity of CaV2.1 and CaV2.2 channels in the control of synaptic strength and presynaptic plasticity.

scholarly journals Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Zohreh Farsi ◽  
Sindhuja Gowrisankaran ◽  
Matija Krunic ◽  
Burkhard Rammner ◽  
Andrew Woehler ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Synaptic Vesicle ◽  
Mouse Brain ◽  
Synaptic Vesicles ◽  
Vacuolar Atpase ◽  
Coated Vesicles ◽  
Electrochemical Gradient ◽  
Proper Timing ◽  
Adenosine Triphosphatases ◽  
Single Vesicle

Newly-formed synaptic vesicles (SVs) are rapidly acidified by vacuolar adenosine triphosphatases (vATPases), generating a proton electrochemical gradient that drives neurotransmitter loading. Clathrin-mediated endocytosis is needed for the formation of new SVs, yet it is unclear when endocytosed vesicles acidify and refill at the synapse. Here, we isolated clathrin-coated vesicles (CCVs) from mouse brain to measure their acidification directly at the single vesicle level. We observed that the ATP-induced acidification of CCVs was strikingly reduced in comparison to SVs. Remarkably, when the coat was removed from CCVs, uncoated vesicles regained ATP-dependent acidification, demonstrating that CCVs contain the functional vATPase, yet its function is inhibited by the clathrin coat. Considering the known structures of the vATPase and clathrin coat, we propose a model in which the formation of the coat surrounds the vATPase and blocks its activity. Such inhibition is likely fundamental for the proper timing of SV refilling.

scholarly journals Neurotransmitter Release Site Replenishment and Presynaptic Plasticity

2020 ◽  
Vol 22 (1) ◽  
pp. 327
Author(s):  
Sumiko Mochida
Keyword(s):  
Neurotransmitter Release ◽  
Synaptic Vesicles ◽  
High Speed ◽  
Release Site ◽  
Short Term ◽  
Short Term Plasticity ◽  
Multiple Protein ◽  
Presynaptic Plasticity ◽  
Presynaptic Plasma Membrane ◽  
Ca2 Channels

An action potential (AP) triggers neurotransmitter release from synaptic vesicles (SVs) docking to a specialized release site of presynaptic plasma membrane, the active zone (AZ). The AP simultaneously controls the release site replenishment with SV for sustainable synaptic transmission in response to incoming neuronal signals. Although many studies have suggested that the replenishment time is relatively slow, recent studies exploring high speed resolution have revealed SV dynamics with milliseconds timescale after an AP. Accurate regulation is conferred by proteins sensing Ca2+ entering through voltage-gated Ca2+ channels opened by an AP. This review summarizes how millisecond Ca2+ dynamics activate multiple protein cascades for control of the release site replenishment with release-ready SVs that underlie presynaptic short-term plasticity.

scholarly journals Control of neurotransmitter release by two distinctmembrane-binding faces of the Munc13-1 C­1C2B region

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Marcial Camacho ◽  
Bradley Quade ◽  
Thorsten Trimbuch ◽  
Junjie Xu ◽  
Levent Sari ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Neurotransmitter Release ◽  
Synaptic Vesicles ◽  
Point Mutations ◽  
Short Term ◽  
In Vitro Reconstitution ◽  
Presynaptic Plasticity ◽  
Hippocampal Cultures

Munc13-1 plays a central role in neurotransmitter release through its conserved C-terminal region, which includes a diacyglycerol (DAG)-binding C1 domain, a Ca2+/PIP2-binding C2B domain, a MUN domain and a C2C domain. Munc13-1 was proposed to bridge synaptic vesicles to the plasma membrane through distinct interactions of the C­1C2B region with the plasma membrane: i) one involving a polybasic face that is expected to yield a perpendicular orientation of Munc13-1 and hinder release; and ii) another involving the DAG-Ca2+-PIP2-binding face that is predicted to result in a slanted orientation and facilitate release. Here we have tested this model and investigated the role of the C­1C2B region in neurotransmitter release. We find that K603E or R769E point mutations in the polybasic face severely impair Ca2+-independent liposome bridging and fusion in in vitro reconstitution assays, and synaptic vesicle priming in primary murine hippocampal cultures. A K720E mutation in the polybasic face and a K706E mutation in the C2B domain Ca2+-binding loops have milder effects in reconstitution assays and do not affect vesicle priming, but enhance or impair Ca2+-evoked release, respectively. The phenotypes caused by combining these mutations are dominated by the K603E and R769E mutations. Our results show that the C1-C2B region of Munc13-1 plays a central role in vesicle priming and support the notion that two distinct faces of this region control neurotransmitter release and short-term presynaptic plasticity.

CYCLIC AMP AND PHOSPHODIESTERASE IN SYNAPTIC VESICLES FROM MOUSE BRAIN

1973 ◽  
Vol 20 (5) ◽  
pp. 1387-1392 ◽  
Author(s):  
G. A. Johnson ◽  
Sally J. Boukma ◽  
R. A. Lahti ◽  
J. Mathews
Keyword(s):  
Cyclic Amp ◽  
Mouse Brain ◽  
Synaptic Vesicles

scholarly journals Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C1C2BMUN

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Junjie Xu ◽  
Marcial Camacho ◽  
Yibin Xu ◽  
Victoria Esser ◽  
Xiaoxia Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Neurotransmitter Release ◽  
Synaptic Vesicles ◽  
Plasma Membranes ◽  
Helical Structure ◽  
Membrane Interface ◽  
Short Term ◽  
Presynaptic Plasticity ◽  
Multiple Domains

Munc13–1 acts as a master regulator of neurotransmitter release, mediating docking-priming of synaptic vesicles and diverse presynaptic plasticity processes. It is unclear how the functions of the multiple domains of Munc13–1 are coordinated. The crystal structure of a Munc13–1 fragment including its C1, C2B and MUN domains (C1C2BMUN) reveals a 19.5 nm-long multi-helical structure with the C1 and C2B domains packed at one end. The similar orientations of the respective diacyglycerol- and Ca2+-binding sites of the C1 and C2B domains suggest that the two domains cooperate in plasma-membrane binding and that activation of Munc13–1 by Ca2+ and diacylglycerol during short-term presynaptic plasticity are closely interrelated. Electrophysiological experiments in mouse neurons support the functional importance of the domain interfaces observed in C1C2BMUN. The structure imposes key constraints for models of neurotransmitter release and suggests that Munc13–1 bridges the vesicle and plasma membranes from the periphery of the membrane-membrane interface.

scholarly journals Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene

1999 ◽  
Vol 96 (4) ◽  
pp. 1716-1721 ◽  
Author(s):  
T. B. Cole ◽  
H. J. Wenzel ◽  
K. E. Kafer ◽  
P. A. Schwartzkroin ◽  
R. D. Palmiter
Keyword(s):  
Mouse Brain ◽  
Synaptic Vesicles ◽  
Intact Mouse
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