CALCINEURIN INHIBITION OF DYNAMIN-I GTPASE ACTIVITY COUPLED TO NERVE-TERMINAL DEPOLARIZATION

被引：190

作者：

LIU, JP ^{[1
]}

SIM, ATR ^{[1
]}

ROBINSON, PJ ^{[1
]}

机构：

[1] UNIV NEWCASTLE,NEUROSCI GRP,NEWCASTLE,NSW 2308,AUSTRALIA

来源：

SCIENCE | 1994年 / 265卷 / 5174期

关键词：

D O I：

10.1126/science.8052858

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 Ca2+-sensitive switch for depolarization-evoked synaptic vesicle recycling.

引用

页码：970 / 973

页数：4

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