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Science 12 August 1994:
Vol. 265. no. 5174, pp. 970 - 973
DOI: 10.1126/science.8052858
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Articles

Science, Vol 265, Issue 5174, 970-973
Copyright © 1994 by American Association for the Advancement of Science

articles

Calcineurin inhibition of dynamin I GTPase activity coupled to nerve terminal depolarization

JP Liu, AT Sim, and PJ Robinson

Endocrine Unit, John Hunter Hospital, NSW, Australia.

Dynamin I is a nerve terminal phosphoprotein with intrinsic guanosine triphosphatase (GTPase) activity that is required for endocytosis. Upon depolarization and synaptic vesicle recycling, dynamin I undergoes a rapid dephosphorylation. Dynamin I was found to be a specific high-affinity substrate for calcineurin in vitro. At low concentrations, calcineurin dephosphorylated dynamin I that had been phosphorylated by protein kinase C. The dephosphorylation inhibited dynamin I GTPase activity in vitro and after depolarization of nerve terminals. The effect in nerve terminals was prevented by the calcineurin inhibitor cyclosporin A. This suggests that in nerve terminals, calcineurin serves as a Ca(2+)-sensitive switch for depolarization-evoked synaptic vesicle recycling.


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