Proteolytic maturation of α2δ controls the probability of synaptic vesicular release
- University College London, United Kingdom
Figures
Figure 1
Effect of proteolytic cleavage of α2(3C)δ-1 on vesicular release in presynaptic terminals of hippocampal neurons.
(a) Fluorescence changes in presynaptic terminals of hippocampal neurons expressing vGlut-pHluorin (vG-pHluorin) in response to electrical stimulation. Left panel, mCherry-positive boutons. Three …
Figure 2
The proteolytic cleavage of α2(3C)δ-1 does not affect the readily releasable pool (RRP) in presynaptic terminals of hippocampal neurons.
(a–c) vG-pHluorin responses (mean ± SEM) to 20 AP at 100 Hz (5–6 trial average, 25 to 50 boutons) from presynaptic terminals of neurons co-transfected with empty vector (a), α2(3C)δ-1 (b) or α2(3C)δ-…
Figure 3
Effect of the proteolytic cleavage of α2(3C)δ-1 on delayed vesicular release in presynaptic terminals of hippocampal neurons.
(a) Average vG-pHluorin responses (mean ± SEM) to 20 APs at 100 Hz (5–6 trial average, 25 to 50 boutons) from presynaptic terminals of neurons co-transfected with empty vector (black), α2(3C)δ-1 …
Figure 4
Quantified co-immunoprecipitation of CaV2.2 with cleaved and uncleaved fractions of wild-type α2δ-1 from WCL of tsA-201 cells.
(a) Left panels show WCL input from tsA-201 cells transfected with GFP-CaV2.2 (lanes 1 and 2) or GFP (lane 3), plus β1b and HA-tagged α2δ-1: upper panel, HA-α2δ-1 input; lower panel, CaV2.2-GFP …
Additional files
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Supplementary file 1
- https://doi.org/10.7554/eLife.37507.006
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Transparent reporting form
- https://doi.org/10.7554/eLife.37507.007
