The Water and Salt Research Center, Dept. of Anatomy, Aarhus Univ., Denmark.
Am J Physiol Renal Physiol. 2011 May;300(5):F1062-73. doi: 10.1152/ajprenal.00721.2010. Epub 2011 Feb 9.
The cellular functions of many eukaryotic membrane proteins, including the vasopressin-regulated water channel aquaporin-2 (AQP2), are regulated by posttranslational modifications. In this article, we discuss the experimental discoveries that have advanced our understanding of how posttranslational modifications affect AQP2 function, especially as they relate to the role of AQP2 in the kidney. We review the most recent data demonstrating that glycosylation and, in particular, phosphorylation and ubiquitination are mechanisms that regulate AQP2 activity, subcellular sorting and distribution, degradation, and protein interactions. From a clinical perspective, posttranslational modification resulting in protein misrouting or degradation may explain certain forms of nephrogenic diabetes insipidus. In addition to providing major insight into the function and dynamics of renal AQP2 regulation, the analysis of AQP2 posttranslational modification may provide general clues as to the role of posttranslational modification for regulation of other membrane proteins.
许多真核膜蛋白的细胞功能，包括血管加压素调节的水通道水通道蛋白-2（AQP2），都受到翻译后修饰的调节。本文讨论了促进我们理解翻译后修饰如何影响 AQP2 功能的实验发现，特别是它们与 AQP2 在肾脏中的作用有关。我们回顾了最近的数据，这些数据表明糖基化，特别是磷酸化和泛素化，是调节 AQP2 活性、亚细胞分拣和分布、降解和蛋白质相互作用的机制。从临床角度来看，导致蛋白质错误定向或降解的翻译后修饰可能解释了某些形式的肾性尿崩症。除了为肾脏 AQP2 调节的功能和动态提供重要见解外，对 AQP2 翻译后修饰的分析还可能为翻译后修饰在调节其他膜蛋白方面的作用提供一般线索。
