Chilcote T J, Siow Y L, Schaeffer E, Greengard P, Thiel G
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021.
J Neurochem. 1994 Oct;63(4):1568-71. doi: 10.1046/j.1471-4159.1994.63041568.x.
Synapsins are neuron-specific phosphoproteins associated with small synaptic vesicles in the presynaptic nerve terminal. Synapsin I, which has been demonstrated to bundle F-actin in vitro, has been postulated to regulate neurotransmitter release by cross-linking synaptic vesicles to the actin cytoskeleton. To investigate the possible interaction of synapsin II with actin filaments, we expressed synapsin II in Spodoptera frugiperda and High Five insect cells using a recombinant baculovirus. Purified recombinant synapsin IIa was incubated with F-actin, and bundle formation was evaluated by light scattering and electron microscopy. Synapsin IIa was found to bundle actin filaments. Dose-response curves indicated that synapsin IIa was more potent than synapsin I in bundling actin filaments. These data suggest that synapsin IIa may cross-link synaptic vesicles and actin filaments in the nerve terminal.
突触素是与突触前神经末梢中的小突触囊泡相关的神经元特异性磷蛋白。突触素I已被证实在体外能使F-肌动蛋白成束,据推测它通过将突触囊泡交联到肌动蛋白细胞骨架来调节神经递质释放。为了研究突触素II与肌动蛋白丝的可能相互作用,我们使用重组杆状病毒在草地贪夜蛾和High Five昆虫细胞中表达突触素II。将纯化的重组突触素IIa与F-肌动蛋白一起孵育,并通过光散射和电子显微镜评估成束情况。发现突触素IIa能使肌动蛋白丝成束。剂量反应曲线表明,突触素IIa在使肌动蛋白丝成束方面比突触素I更有效。这些数据表明突触素IIa可能在神经末梢中将突触囊泡与肌动蛋白丝交联起来。