网格蛋白从包被小泡的释放依赖于三磷酸核苷和胞质溶胶组分。
Release of clathrin from coated vesicles dependent upon a nucleoside triphosphate and a cytosol fraction.
作者信息
Patzer E J, Schlossman D M, Rothman J E
出版信息
J Cell Biol. 1982 Apr;93(1):230-6. doi: 10.1083/jcb.93.1.230.
Abstract
Calf-brain coated vesicles were incubated with ATP and a cytosol fraction. As much as 90% of the clathrin was selectively released within 10 min at 37 degrees C without detectable proteolysis. This uncoating process required the presence of both ATP and cytosol. Empty cages of clathrin could also be dissociated in a similar manner. A nonhydrolyzable analogue, 5'-adenylylimidodiphosphate (AMP-PNP), would not substitute for ATP. Clathrin was dissociated from coats in a form unable to reassemble into cages under standard conditions. These reactions may reflect a segment of a clathrin-coated vesicle cycle in which coats are removed from vesicles after budding.
摘要
将小牛脑包被的囊泡与ATP和胞质溶胶组分一起孵育。在37℃下，多达90%的网格蛋白在10分钟内被选择性释放，且未检测到蛋白水解。这种脱包被过程需要ATP和胞质溶胶的存在。空的网格蛋白笼也能以类似方式解离。一种不可水解的类似物5'-腺苷酰亚胺二磷酸（AMP-PNP）不能替代ATP。在标准条件下，网格蛋白以一种无法重新组装成笼的形式从包被中解离。这些反应可能反映了网格蛋白包被囊泡循环的一个阶段，即出芽后从囊泡上移除包被。
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