Matching kinetics of synaptic vesicle recycling and enhanced neurotransmitter influx by Ca2 in brain plasma membrane vesicles

1998 ◽  
Vol 33 (5) ◽  
pp. 399-405 ◽  
Author(s):  
Ilona Kovács ◽  
Éva Szárics ◽  
Gabriella Nyitrai ◽  
Tamás Blandl ◽  
Julianna Kardos
1978 ◽  
Vol 56 (6) ◽  
pp. 921-925
Author(s):  
L. Spero

A technique is described which has enabled us to measure changes in 22Na+ efflux from smooth muscle plasma membrane vesicles. The resting 22Na+ efflux from these sealed vesicles showed a concentration-dependent increase in response to acetylcholine and other muscarinic agonists, in similar concentrations to those which increased 42K+ efflux in whole muscle. The kinetics of this efflux were complex and could not be described by less than three exponential processes. The response to agonists has, therefore, been characterized by measurement of the half-life of 22Na+ efflux (t1/2). The acetylcholine effect was inhibited by atropine, but unlike the situation in the whole muscle, this inhibition was noncompetitive. Tubocuraine (a nicotinic antagonist) had no effect on this acetylcholine response. Atropine has no effect by itself on the resting 22Na+ efflux, neither did tetrodotoxin or ouabain. 22Na+ efflux from erythrocyte ghosts and liposomes, prepared from lipid extracts of the smooth muscle plasma membrane, was not modified by acetylcholine or atropine.


2021 ◽  
Author(s):  
Yuuta Imoto ◽  
Sumana Raychaudhuri ◽  
Pascal Fenske ◽  
Eduardo Sandoval ◽  
Kie Itoh ◽  
...  

SummaryDynamin mediates fission of vesicles from the plasma membrane during endocytosis. Typically, dynamin is recruited from the cytosol to endocytic sites, requiring seconds to tens of seconds. However, ultrafast endocytosis in neurons internalizes vesicles as quickly as 50 ms during synaptic vesicle recycling. Here we demonstrate that Dynamin 1 is pre-recruited to endocytic sites for ultrafast endocytosis. Specifically, Dynamin 1xA, a splice variant of Dynamin 1, interacts with Syndapin 1 to form molecular condensates on the plasma membrane when the proline-rich domain of this variant is dephosphorylated. When this domain is mutated to include phosphomimetic residues or Syndapin 1’s dynamin-interacting domain is mutated, Dynamin 1xA becomes diffuse, and consequently, ultrafast endocytosis slows down by ∼100-fold. Mechanistically, Syndapin 1 acts as an adaptor by binding the plasma membrane and stores Dynamin 1xA at endocytic sites. This cache bypasses the recruitment step and accelerates endocytosis at synapses.


Neuron ◽  
1993 ◽  
Vol 11 (4) ◽  
pp. 713-724 ◽  
Author(s):  
Timothy A. Ryan ◽  
Harald Reuter ◽  
Beverly Wendland ◽  
Felix E. Schweizer ◽  
Richard W. Tsien ◽  
...  

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 1734 ◽  
Author(s):  
Natali L. Chanaday ◽  
Ege T. Kavalali

Synaptic vesicle recycling is essential for sustained and reliable neurotransmission. A key component of synaptic vesicle recycling is the synaptic vesicle biogenesis process that is observed in synapses and that maintains the molecular identity of synaptic vesicles. However, the mechanisms by which synaptic vesicles are retrieved and reconstituted after fusion remain unclear. The complex molecular composition of synaptic vesicles renders their rapid biogenesis a daunting task. Therefore, in this context, kiss-and-run type transient fusion of synaptic vesicles with the plasma membrane without loss of their membrane composition and molecular identity remains a viable hypothesis that can account for the fidelity of the synaptic vesicle cycle. In this article, we discuss the biological implications of this problem as well as its possible molecular solutions.


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