Dynamin I phosphorylation by GSK3 controls activity-dependent bulk endocytosis of synaptic vesicles

@inproceedings{Clayton2010DynaminIP,
  title={Dynamin I phosphorylation by GSK3 controls activity-dependent bulk endocytosis of synaptic vesicles},
  author={E Clayton and Nancy Sue and K. J. Smillie and Timothy R. O’Leary and N. Bache and Giselle Cheung and A. R. Cole and D. J Wyllie and Calum Sutherland and P J Robinson and M. A Cousin},
  booktitle={Nature Neuroscience},
  year={2010}
}
Glycogen synthase kinase 3 (GSK3) is a critical enzyme in neuronal physiology; however, it is not yet known whether it has any specific role in presynaptic function. We found that GSK3 phosphorylates a residue on the large GTPase dynamin I (Ser-774) both in vitro and in primary rat neuronal cultures. This was dependent on prior phosphorylation of Ser-778 by cyclin-dependent kinase 5. Using both acute inhibition with pharmacological antagonists and silencing of expression with short hairpin RNA… CONTINUE READING
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