Multiple domains in caveolin-1 control its intracellular traffic.

Multiple domains in caveolin-1 control its intracellular traffic.
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DOI:
10.1083/jcb.148.1.17
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发表时间:
2000-01-10
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Anderson RG
Anderson RG
中科院分区:
其他
文献类型:
--
作者:
Machleidt T;Li WP;Liu P;Anderson RG

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小窝蛋白-1是小窝的一种膜蛋白,在胆固醇向小窝的转运和调节该位点多种信号分子的活性中起重要作用。该分子在内质网中合成,运输到细胞表面,并经历了一个知之甚少的再循环行程。我们已经使用诱变来确定控制小窝蛋白-1从其合成位点到细胞表面的交通的分子的部分。我们确定了四个区域的分子,似乎影响小窝蛋白-1交通。氨基酸66和70之间的区域是该分子最保守的区域,是离开内质网所必需的。氨基酸71和80之间的区域控制将小窝蛋白-1低聚物掺入高尔基体的耐洗涤剂区域。氨基酸91-100和134-154都控制寡聚化并离开高尔基体。去除分子的其他部分对新合成的小窝蛋白-1靶向小窝没有影响。结果表明,小窝蛋白-1在不同的内膜隔室之间的运动是由多个步骤控制的。
Caveolin-1 is an integral membrane protein of caveolae that is thought to play an important role in both the traffic of cholesterol to caveolae and modulating the activity of multiple signaling molecules at this site. The molecule is synthesized in the endoplasmic reticulum, transported to the cell surface, and undergoes a poorly understood recycling itinerary. We have used mutagenesis to determine the parts of the molecule that control traffic of caveolin-1 from its site of synthesis to the cell surface. We identified four regions of the molecule that appear to influence caveolin-1 traffic. A region between amino acids 66 and 70, which is in the most conserved region of the molecule, is necessary for exit from the endoplasmic reticulum. The region between amino acids 71 and 80 controls incorporation of caveolin-1 oligomers into detergent-resistant regions of the Golgi apparatus. Amino acids 91–100 and 134–154 both control oligomerization and exit from the Golgi apparatus. Removal of other portions of the molecule has no effect on targeting of newly synthesized caveolin-1 to caveolae. The results suggest that movement of caveolin-1 among various endomembrane compartments is controlled at multiple steps.
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