INTERACTION OF FREE AND SYNAPTIC VESICLE BOUND SYNAPSIN-I WITH F-ACTIN
INTERACTION OF FREE AND SYNAPTIC VESICLE BOUND SYNAPSIN-I WITH F-ACTIN
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DOI：
10.1016/0896-6273(92)90303-u
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发表时间：
1992-02-01
期刊：
影响因子：
16.2
通讯作者：
GREENGARD, P
中科院分区：
文献类型：
--
作者：
BENFENATI, F;VALTORTA, F;GREENGARD, P
突触蛋白I是一种神经元特异性磷酸化蛋白，以磷酸化依赖的方式与小突触囊泡和f -肌动蛋白结合。我们发现突触蛋白1去磷酸化诱导肌动蛋白丝数量的剂量依赖性增加，在高离子强度下，肌动蛋白丝被突触蛋白1磷酸化所消除。纤维数量的增加似乎是由于突触素1的成核作用，而不是由于钩端盖/切断活动。突触囊泡结合突触蛋白I与自由突触蛋白I在增加纤维数量方面同样有效。这些数据支持了突触蛋白I参与外胞吞周期中肌动蛋白网络动力学调节的观点。
Synapsin I is a neuron-specific phosphoprotein that binds to small synaptic vesicles and F-actin in a phosphorylation-dependent fashion. We have found that dephosphorylated synapsin I induces a dose-dependent increase in the number of actin filaments, which at high ionic strength is abolished by synapsin I phosphorylation. The increase in filament number appears to be due to a nucleating effect of synapsin I and not to a barbed-end capping/severing activity. Synaptic vesicle-bound synapsin I was as effective as free synapsin I in increasing the number of filaments. These data support the view that synapsin I is involved in the regulation of the dynamics of the actin-based network during the exo-endocytotic cycle.