Retention of secretory proteins in an intermediate compartment and disappearance of the Golgi complex in an END4 mutant of Chinese hamster ovary cells.
Retention of secretory proteins in an intermediate compartment and disappearance of the Golgi complex in an END4 mutant of Chinese hamster ovary cells.
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DOI：
10.1083/jcb.117.4.701
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发表时间：
1992-05
期刊：
影响因子：
--
通讯作者：
Draper RK
中科院分区：
文献类型：
--
作者：
Kao CY;Draper RK
突变体 V.24.1 是温度敏感 CHO 细胞 End4 互补组的成员，在限制温度下分泌有缺陷（Wang, R.-H.、P. A. Colbaugh、C.-Y. Kao、E. A. Rutledge 和 R. K. Draper. 1990. J. Biol. Chem. 265:20179-20187；Presley, J. F.、R.K.Draper 和 D.T.Brown，1991。J.Virol，65：1332-1339）。我们进一步研究了分泌性病变并报告了三个主要发现。首先，分泌受阻并不是由于内质网中分泌蛋白的异常折叠或寡聚化，因为流感病毒的血凝素在限制温度下在突变体和亲本细胞中以相同的速率折叠和寡聚化。其次，分泌蛋白积聚在内质网和高尔基体之间的隔室中。几条证据支持这一结论，最直接的是通过免疫荧光显微镜观察流感病毒血凝素与已知存在于中间隔室中的 58-kD 蛋白质的共定位。第三，在荧光显微镜的分辨率下，突变细胞中的高尔基复合体在限制温度下消失。
Mutant V.24.1, a member of the End4 complementation group of temperature-sensitive CHO cells, is defective in secretion at the restrictive temperature (Wang, R.-H., P. A. Colbaugh, C.-Y. Kao, E. A. Rutledge, and R. K. Draper. 1990. J. Biol. Chem. 265:20179-20187; Presley, J. F., R. K. Draper, and D. T. Brown. 1991. J. Virol. 65:1332- 1339). We have further investigated the secretory lesion and report three main findings. First, the block in secretion is not due to aberrant folding or oligomerization of secretory proteins in the endoplasmic reticulum because the hemagglutinin of influenza virus folded and oligomerized at the same rate in mutant and parental cells at the restrictive temperature. Second, secretory proteins accumulated in a compartment intermediate between the ER and the Golgi. Several lines of evidence support this conclusion, the most direct being the colocalization by immunofluorescence microscopy of influenza virus hemagglutinin with a 58-kD protein that is known to reside in an intermediate compartment. Third, at the resolution of fluorescence microscopy, the Golgi complex in the mutant cells vanished at the restrictive temperature.