Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells.

@article{Nili2006Munc181PB,
  title={Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells.},
  author={U Nili and H. G. M. de Wit and Attila Guly{\'a}s-Kov{\'a}cs and Ruud F.G. Toonen and Jakob Balslev S\orensen and Matthijs Verhage and Uri Ashery},
  journal={Neuroscience},
  year={2006},
  volume={143 2},
  pages={487-500}
}
Activation of protein kinase C (PKC) after robust stimulation is necessary for vesicle pool replenishment in secretory cells. Here we studied the contribution of a prominent downstream PKC target, Munc18-1, to this process in bovine chromaffin cells. In these cells, both activation of endogenous PKC and overexpressing of Munc18-1 promote vesicle pool replenishment after an extensive stimulation. In order to study the physiological relevance of PKC-dependent Munc18-1 phosphorylation, we… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 37 extracted citations

PKC-2 phosphorylation of UNC-18 Ser322 in AFD neurons regulates temperature dependency of locomotion.

The Journal of neuroscience : the official journal of the Society for Neuroscience • 2012
View 4 Excerpts
Highly Influenced

Exocytosis proteins as novel targets for diabetes prevention and/or remediation?

American journal of physiology. Regulatory, integrative and comparative physiology • 2017

Millisecond Ca2+ dynamics activate multiple protein cascades for synaptic vesicle control

Proceedings of the Japan Academy. Series B, Physical and biological sciences • 2017

Phosphorylation of synaptotagmin-1 controls a post-priming step in PKC-dependent presynaptic plasticity.

Proceedings of the National Academy of Sciences of the United States of America • 2016

Similar Papers

Loading similar papers…