Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels
Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels
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DOI：
10.1016/s0962-8924(98)01491-3
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发表时间：
1999-03-01
影响因子：
19
通讯作者：
Hicke, L
中科院分区：
文献类型：
--
作者：
Hicke, L
酿酒酵母中的g蛋白偶联受体和转运体被泛素修饰以响应配体结合。在大多数情况下，蛋白酶体不能识别这些泛素化蛋白。相反，泛素化作用触发溶酶体样液泡内质膜蛋白的内化和降解。许多哺乳动物受体和至少一个离子通道在质膜上发生泛素化，这种修饰是它们下调所必需的。其中一些细胞表面蛋白似乎可以被蛋白酶体和溶酶体蛋白酶降解。最近的证据表明，受体内化所需的其他蛋白质也可能受到泛素化的调节，这表明泛素在调节质膜蛋白活性方面发挥着不同的作用。
G-protein-coupled receptors and transporters in Saccharomyces cerevisiae are modified with ubiquitin in response to ligand binding. In most cases, the proteasome does not recognize these ubiquitinated proteins. Instead, ubiquitination serves to trigger internalization and degradation of plasma membrane proteins in the lysosome-like vacuole. A number of mammalian receptors and at least one ion channel undergo ubiquitination at the plasma membrane, and this modification is required for their downregulation. Some of these cell-surface proteins appear to be degraded by both the proteasome and lysosomal proteases. Recent evidence indicates that other proteins required for receptor internalization might also be regulated by ubiquitination, suggesting that ubiquitin plays diverse roles in regulating plasma membrane protein activity.