Chieregatti E, Ceccaldi P E, Benfenati F, Valtorta F
Dept. of Medical Pharmacology, University of Milan, Italy.
FEBS Lett. 1996 Dec 2;398(2-3):211-6. doi: 10.1016/s0014-5793(96)01240-9.
We have analyzed the effects of synaptic vesicles on actin polymerization by using a time-resolved spectrofluorometric assay. We have found that synaptic vesicles have complex effects on the kinetics of actin polymerization, which vary depending on whether the synaptic vesicle-specific phosphoprotein synapsin I is absent or present on their membrane. Synapsin I bound either to synaptic vesicles or to pure phospholipid vesicles exhibits phosphorylation-dependent actin-nucleating activity. Synaptic vesicles depleted of endogenous synapsin I decrease the rate and the final extent of actin polymerization, an effect which is not observed with pure phospholipid vesicles. Thus, the state of association of synapsin I with synaptic vesicles, which is modulated by its state of phosphorylation, may affect actin assembly and the physico-chemical characteristics of the synaptic vesicle microenvironment.
我们通过时间分辨荧光光谱分析法分析了突触小泡对肌动蛋白聚合的影响。我们发现,突触小泡对肌动蛋白聚合动力学具有复杂的影响,这种影响取决于突触小泡特异性磷蛋白突触素I在其膜上是否存在。结合在突触小泡或纯磷脂小泡上的突触素I表现出磷酸化依赖性的肌动蛋白成核活性。耗尽内源性突触素I的突触小泡会降低肌动蛋白聚合的速率和最终程度,而纯磷脂小泡则未观察到这种效应。因此,突触素I与突触小泡的结合状态受其磷酸化状态的调节,可能会影响肌动蛋白组装以及突触小泡微环境的物理化学特性。