Dihydropyrazole Insecticides: Interference with Depolarization-Dependent Phosphorylation of Synapsin I and Evoked Release ofl-Glutamate in Nerve-Terminal Preparations from Mammalian Brain

1996 ◽  
Vol 54 (1) ◽  
pp. 24-30 ◽  
Author(s):  
Aiguo Zhang ◽  
Paul Towner ◽  
Russell A. Nicholson
Keyword(s):  
Nerve Terminal ◽  
Mammalian Brain ◽  
Synapsin I

scholarly journals Synapsin I Is a Major Endogenous Substrate for Protein L-Isoaspartyl Methyltransferase in Mammalian Brain

2006 ◽  
Vol 281 (13) ◽  
pp. 8389-8398 ◽  
Author(s):  
Kathryn J. Reissner ◽  
Mallik V. Paranandi ◽  
Trang M. Luc ◽  
Hester A. Doyle ◽  
Mark J. Mamula ◽  
...  
Keyword(s):  
Mammalian Brain ◽  
Synapsin I ◽  
Protein L ◽  
Endogenous Substrate ◽  
Isoaspartyl Methyltransferase

scholarly journals Collagen-derived matricryptins promote inhibitory nerve terminal formation in the developing neocortex

2016 ◽  
Vol 212 (6) ◽  
pp. 721-736 ◽  
Author(s):  
Jianmin Su ◽  
Jiang Chen ◽  
Kumiko Lippold ◽  
Aboozar Monavarfeshani ◽  
Gabriela Lizana Carrillo ◽  
...  
Keyword(s):  
Neuronal Activity ◽  
Nerve Terminal ◽  
Inhibitory Synapses ◽  
Mammalian Brain ◽  
Nerve Terminals ◽  
Brain Disorders ◽  
Integrin Receptors ◽  
Developing Neocortex ◽  
Cortical Circuit ◽  
Circuit Formation

Inhibitory synapses comprise only ∼20% of the total synapses in the mammalian brain but play essential roles in controlling neuronal activity. In fact, perturbing inhibitory synapses is associated with complex brain disorders, such as schizophrenia and epilepsy. Although many types of inhibitory synapses exist, these disorders have been strongly linked to defects in inhibitory synapses formed by Parvalbumin-expressing interneurons. Here, we discovered a novel role for an unconventional collagen—collagen XIX—in the formation of Parvalbumin+ inhibitory synapses. Loss of this collagen results not only in decreased inhibitory synapse number, but also in the acquisition of schizophrenia-related behaviors. Mechanistically, these studies reveal that a proteolytically released fragment of this collagen, termed a matricryptin, promotes the assembly of inhibitory nerve terminals through integrin receptors. Collectively, these studies not only identify roles for collagen-derived matricryptins in cortical circuit formation, but they also reveal a novel paracrine mechanism that regulates the assembly of these synapses.

scholarly journals Dephosphorylated synapsin I anchors synaptic vesicles to actin cytoskeleton: an analysis by videomicroscopy.

1995 ◽  
Vol 128 (5) ◽  
pp. 905-912 ◽  
Author(s):  
P E Ceccaldi ◽  
F Grohovaz ◽  
F Benfenati ◽  
E Chieregatti ◽  
P Greengard ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Synaptic Vesicle ◽  
Nerve Terminal ◽  
Actin Filaments ◽  
Neurotransmitter Release ◽  
Synaptic Vesicles ◽  
Actin Polymerization ◽  
Synapsin I ◽  
Cam Kinase Ii ◽  
Cam Kinase

Synapsin I is a synaptic vesicle-associated protein which inhibits neurotransmitter release, an effect which is abolished upon its phosphorylation by Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). Based on indirect evidence, it was suggested that this effect on neurotransmitter release may be achieved by the reversible anchoring of synaptic vesicles to the actin cytoskeleton of the nerve terminal. Using video-enhanced microscopy, we have now obtained experimental evidence in support of this model: the presence of dephosphorylated synapsin I is necessary for synaptic vesicles to bind actin; synapsin I is able to promote actin polymerization and bundling of actin filaments in the presence of synaptic vesicles; the ability to cross-link synaptic vesicles and actin is specific for synapsin I and is not shared by other basic proteins; the cross-linking between synaptic vesicles and actin is specific for the membrane of synaptic vesicles and does not reflect either a non-specific binding of membranes to the highly surface active synapsin I molecule or trapping of vesicles within the thick bundles of actin filaments; the formation of the ternary complex is virtually abolished when synapsin I is phosphorylated by CaM kinase II. The data indicate that synapsin I markedly affects synaptic vesicle traffic and cytoskeleton assembly in the nerve terminal and provide a molecular basis for the ability of synapsin I to regulate the availability of synaptic vesicles for exocytosis and thereby the efficiency of neurotransmitter release.

scholarly journals Active presynaptic ribosomes in mammalian brain nerve terminals, and increased transmitter release after protein synthesis inhibition

2018 ◽  
Author(s):  
Matthew S. Scarnati ◽  
Rahul Kataria ◽  
Mohana Biswas ◽  
Kenneth G. Paradiso
Keyword(s):  
Protein Synthesis ◽  
Nerve Terminal ◽  
Brain Slices ◽  
Mammalian Brain ◽  
Nerve Terminals ◽  
Local Translation ◽  
Vesicle Recycling ◽  
Presynaptic Vesicle ◽  
Presynaptic Nerve Terminals ◽  
Presynaptic Protein

AbstractPresynaptic neuronal activity requires the localization of thousands of proteins that are typically synthesized in the soma and transported to nerve terminals. Local translation for some dendritic proteins occurs, but local translation in mammalian presynaptic nerve terminals is difficult to demonstrate. Here, we present evidence for local presynaptic protein synthesis in the mammalian brain at a glutamatergic nerve terminal. We show an essential ribosomal component, 5.8s rRNA, in terminals. We also show active translation in nerve terminals, in situ, in brain slices demonstrating ongoing presynaptic protein synthesis. After inhibiting translation for ~1 hour, the presynaptic terminal exhibits increased spontaneous release, and increased evoked release with an increase in vesicle recycling during stimulation trains. Postsynaptic response, shape and amplitude were not affected. We conclude that ongoing protein synthesis limits vesicle release at the nerve terminal which reduces the need for presynaptic vesicle replenishment, thus conserving energy required for maintaining synaptic transmission.

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