Brodin L, Löw P, Shupliakov O
Department of Neuroscience, The Nobel Institute for Neurophysiology, Karolinska Institutet, Stockholm, S-171 77, Sweden.
Curr Opin Neurobiol. 2000 Jun;10(3):312-20. doi: 10.1016/s0959-4388(00)00097-0.
Synaptic vesicles are recycled with remarkable speed and precision in nerve terminals. A major recycling pathway involves clathrin-mediated endocytosis at endocytic zones located around sites of release. Different 'accessory' proteins linked to this pathway have been shown to alter the shape and composition of lipid membranes, to modify membrane-coat protein interactions, and to influence actin polymerization. These include the GTPase dynamin, the lysophosphatidic acid acyl transferase endophilin, and the phosphoinositide phosphatase synaptojanin. Protein perturbation studies in living nerve terminals are now beginning to link the actions of these proteins with morphologically defined steps of endocytosis.
突触小泡在神经末梢以惊人的速度和精度进行循环利用。一条主要的循环途径涉及在释放位点周围的内吞区域通过网格蛋白介导的内吞作用。已表明与该途径相关的不同“辅助”蛋白可改变脂质膜的形状和组成,修饰膜衣蛋白相互作用,并影响肌动蛋白聚合。这些蛋白包括GTP酶发动蛋白、溶血磷脂酸酰基转移酶内吞蛋白,以及磷酸肌醇磷酸酶突触素。对活神经末梢进行的蛋白质干扰研究如今开始将这些蛋白的作用与形态学上明确的内吞步骤联系起来。