Expression of a neuromodulin-?-galactosidase fusion protein in primary cultured neurons and its accumulation in growth cones

1991 ◽  
Vol 104 (1-2) ◽  
Author(s):  
Yuechueng Liu ◽  
DanielR. Storm
2017 ◽  
Vol 14 (11) ◽  
Author(s):  
Ping Wang ◽  
Keliang Chen ◽  
Yuehua Gu ◽  
Qihao Guo ◽  
Zhen Hong ◽  
...  

1997 ◽  
Vol 28 ◽  
pp. S104
Author(s):  
Hiroshi Ohnishi ◽  
Misae Kubota ◽  
Shin-Ichiro Sano

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Quentin Bourgeois-Jaarsma ◽  
Matthijs Verhage ◽  
Alexander J. Groffen

Abstract Communication between neurons involves presynaptic neurotransmitter release which can be evoked by action potentials or occur spontaneously as a result of stochastic vesicle fusion. The Ca2+-binding double C2 proteins Doc2a and –b were implicated in spontaneous and asynchronous evoked release, but the mechanism remains unclear. Here, we compared wildtype Doc2b with two Ca2+ binding site mutants named DN and 6A, previously classified as gain- and loss-of-function mutants. They carry the substitutions D218,220N or D163,218,220,303,357,359A respectively. We found that both mutants bound phospholipids at low Ca2+ concentrations and were membrane-associated in resting neurons, thus mimicking a Ca2+-activated state. Their overexpression in hippocampal primary cultured neurons had similar effects on spontaneous and evoked release, inducing high mEPSC frequencies and increased short-term depression. Together, these data suggest that the DN and 6A mutants both act as gain-of-function mutants at resting conditions.


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