GUANINE-NUCLEOTIDES MODULATE THE EFFECTS OF BREFELDIN-A IN SEMIPERMEABLE CELLS - REGULATION OF THE ASSOCIATION OF A 110-KD PERIPHERAL MEMBRANE-PROTEIN WITH THE GOLGI-APPARATUS
GUANINE-NUCLEOTIDES MODULATE THE EFFECTS OF BREFELDIN-A IN SEMIPERMEABLE CELLS - REGULATION OF THE ASSOCIATION OF A 110-KD PERIPHERAL MEMBRANE-PROTEIN WITH THE GOLGI-APPARATUS
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DOI：
10.1083/jcb.112.4.579
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发表时间：
1991-02-01
影响因子：
7.8
通讯作者：
KLAUSNER, RD
中科院分区：
文献类型：
--
作者：
DONALDSON, JG;LIPPINCOTTSCHWARTZ, J;KLAUSNER, RD
110 kD外周膜蛋白从高尔基体的释放是布雷菲德菌素A（BFA）作用的早期事件，在高尔基体膜进入ER的运动之前。ATP耗竭也导致可逆的重新分配的110 kD蛋白质从高尔基体膜进入胞质溶胶，虽然没有高尔基体解体发生。 为了进一步确定BFA对110-kD蛋白与高尔基体的关联的影响，我们使用过滤器穿孔技术来产生半透性细胞。 所有以前观察到的影响，包括快速重新分配的110-kD蛋白质和高尔基体膜进入ER的运动，可以重现在半透性细胞。 使用GTP的不可水解类似物GTP-γ-S研究了鸟嘌呤核苷酸在此过程中的作用。 用GTP-γ-S预处理半透性细胞防止了BFA诱导的110-kD蛋白从高尔基体和高尔基体膜进入ER的运动的重新分配。 GTP-γ-S也可以消除观察到的110-kD蛋白从高尔基体膜的释放，这发生在响应ATP耗竭。 此外，当110-kD的蛋白质已首先从高尔基体膜上解离ATP耗竭，GTP-γ-S可以恢复高尔基体膜协会的110-kD蛋白质，但如果没有BFA存在。 在半透性细胞中观察到的GTP-γ-S的所有这些作用可以在用AlF 4-处理的完整细胞中重现。 这些结果表明，鸟嘌呤核苷酸调节的动态协会/解离的110-kD蛋白质与高尔基体和BFA干扰这一过程的干扰与协会的110-kD蛋白质与高尔基体。
The release of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A (BFA) action, preceding the movement of Golgi membrane into the ER. ATP depletion also causes the reversible redistribution of the 110-kD protein from Golgi membrane into the cytosol, although no Golgi disassembly occurs. To further define the effects of BFA on the association of the 110-kD protein with the Golgi apparatus we have used filter perforation techniques to produce semipermeable cells. All previously observed effects of BFA, including the rapid redistribution of the 110-kD protein and the movement of Golgi membrane into the ER, could be reproduced in the semipermeable cells. The role of guanine nucleotides in this process was investigated using the nonhydrolyzable analogue of GTP, GTP-gamma-S. Pretreatment of semipermeable cells with GTP-gamma-S prevented the BFA-induced redistribution of the 110-kD protein from the Golgi apparatus and movement of Golgi membrane into the ER. GTP-gamma-S could also abrogate the observed release of the 110-kD protein from Golgi membranes which occurred in response to ATP depletion. Additionally, when the 110-kD protein had first been dissociated from Golgi membranes by ATP depletion, GTP-gamma-S could restore Golgi membrane association of the 110-kD protein, but not if BFA was present. All of these effects observed with GTP-gamma-S in semipermeable cells could be reproduced in intact cells treated with AlF4-. These results suggest that guanine nucleotides regulate the dynamic association/dissociation of the 110-kD protein with the Golgi apparatus and that BFA perturbs this process by interfering with the association of the 110-kD protein with the Golgi apparatus.