Chaudhry FA, Reimer RJ, Bellocchio EE, Danbolt NC, Osen KK, Edwards RH, Storm - Mathisen J (1998) The vesicular GABA transporter, VGAT, localizes to
synaptic vesicles in sets of glycinergic as well as GABAergic neurons J Neurosci, 18 (23), 9733 - 50 PubMed 9822734
Whittaker was the scientist who first isolated
synaptic vesicles in the 1960s.
Not exact matches
During
synaptic vesicle fusion, the soluble N - ethylmaleimide - sensitive factor — attachment protein receptor (SNARE) protein syntaxin - 1 exhibits two conformations that both bind to Munc18 - 1: a «closed» conformation outside the SNARE complex and an «open» conformation
in the SNARE complex.
We generated knockout mice lacking synaptobrevin / VAMP 2, the vesicular SNARE protein responsible for
synaptic vesicle fusion
in forebrain synapses, to make use of the exquisite temporal resolution of electrophysiology
in measuring fusion.
Fluorescently labeled
synaptic vesicles inside the axons of cultured neurons were recorded with stimulated emission depletion (STED) microscopy
in a 2.5 - micrometer by 1.8 - micrometer field of view.
In addition, synapsin II suppression resulted in a selective decrease in the amounts of several synaptic vesicle - associated protein
In addition, synapsin II suppression resulted
in a selective decrease in the amounts of several synaptic vesicle - associated protein
in a selective decrease
in the amounts of several synaptic vesicle - associated protein
in the amounts of several
synaptic vesicle - associated proteins.
I ache to see your action potential
in action To be blinded by the searing speed of your electric signal As it sparks from node to node To behold the violent beauty of
vesicles fusing with your presynaptic membrane — Pouring their contents into your
synaptic cleft How I wish to be your postsynaptic cell So that I may be flooded by your molecules
The structure of synaptophysin suggests that the protein may function as a channel
in the
synaptic vesicle membrane, with the carboxyl terminus serving as a binding site for cellular factors.
We now know that each quantum, consisting of a collection of around 5000 transmitter molecules, is contained
in a little round organelle
in the presynaptic terminal that Sanford Palay and George Palade had earlier discovered and called the «
synaptic vesicl.e» Neurotransmitter is released from these
synaptic vesicles to the outside of the neuron
in response to the influx of Ca2 + into the presynaptic terminal.
During this time, we together with our long - time collaborators Reinhard Jahn and Jose Rizo, and
in parallel with Richard Scheller and others, discovered the role of SNARE and SM proteins
in synaptic vesicle fusion.
Beginning
in 1988 Scheller, then at Stanford, succeeded
in characterizing several key proteins necessary for
synaptic vesicle fusion with the presynaptic membrane, the prerequisite step for neurotransmitter release.
«If you inhibit [endocytosis
in the nerve terminal], then the
vesicle recycling becomes slower and the supply of the
vesicles is inhibited,» OIST Professor Tomoyuki Takahashi from the Cellular and Molecular
Synaptic Function Unit explains.
The study involved lab - based experiments
in which synthetic
vesicles, modelling the
synaptic vesicles found the brain, were exposed to alpha - synuclein.
«It is a sort of shepherding effect by alpha - synuclein that occurs away from the synapse itself, and controls the number of
synaptic vesicles used
in each transmission,» Fusco said.
To determine whether the protein
in question, at the time known as BNPI, mediated the transport of glutamate into
synaptic vesicles, the researchers inserted the BNPI DNA into rat cells that normally lacked BNPI protein.
Discrete Residues
in the C < sub > 2 B Domain of Synaptotagmin I Independently Specify Endocytic Rate and
Synaptic Vesicle Size.
Roles of BLOC - 1 and adaptor protein - 3 complexes
in cargo sorting to
synaptic vesicles.
While neurotransmitters are created
in the interior of the cell, they are pumped,
in large quantity, into
synaptic vesicles tucked into the wall of a nerve cell's so - called «terminal,» the launch pad from which chemical messages are released from the cell.
In particular, he characterized the first
synaptic vesicle membrane associated protein, v - SNARE or VAMP, and the first plasma membrane associated target proteins, t - SNAREs or syntaxin and SNAP - 25.
Richard Scheller has used a combination of biochemistry, molecular biology, and cell biology to identify several key
synaptic vesicle and plasma membrane proteins involved
in fusion of the neurotransmitter - containing
vesicles with the membrane of the presynaptic terminal.
Remarkably, there was no difference
in energy levels between the two, and both types of boutons had sufficient ATP to support
synaptic vesicle cycling.
«You wouldn't have time
in the speed required for
synaptic transmission to make the
vesicles, load them up, and put them
in the active zone ready to release them.
In the late 1990s, he and Reinhard Jahn, now at the Max Planck Institute of Biophysical Chemistry, determined the structures of some of the key proteins and complexes involved in the process of synaptic vesicle fusio
In the late 1990s, he and Reinhard Jahn, now at the Max Planck Institute of Biophysical Chemistry, determined the structures of some of the key proteins and complexes involved
in the process of synaptic vesicle fusio
in the process of
synaptic vesicle fusion.
The identification of proteins, VGLUT1 - 3 (Neuron 2001, PNAS 2002), that pump glutamate into
synaptic vesicles allows the packaging of the transmitter to be characterised
in health and disease (J Comp Neurol 2004, 2006, 2007) and modified by gene knock - out (Science 2004).