水通道蛋白-2转运及其结合蛋白复合物的调控
Regulation of aquaporin-2 trafficking and its binding protein complex.
作者信息
Noda Yumi, Sasaki Sei
机构信息
Department of Nephrology, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Tokyo 113-8519, Japan.
出版信息
Biochim Biophys Acta. 2006 Aug;1758(8):1117-25. doi: 10.1016/j.bbamem.2006.03.004. Epub 2006 Mar 31.
Trafficking of water channel aquaporin-2 (AQP2) to the apical membrane is critical to water reabsorption in renal collecting ducts and its regulation maintains body water homeostasis. However, exact molecular mechanisms which recruit AQP2 are unknown. Recent studies highlighted a key role for spatial and temporal regulation of actin dynamics in AQP2 trafficking. We have recently identified AQP2-binding proteins which directly regulate this trafficking: SPA-1, a GTPase-activating protein (GAP) for Rap1, and cytoskeletal protein actin. In addition, a multiprotein "force generator" complex which directly binds to AQP2 has been discovered. This review summarizes recent advances related to the mechanism for AQP2 trafficking.
水通道蛋白-2（AQP2）向顶端膜的转运对于肾集合管中的水重吸收至关重要，其调节维持着机体水平衡。然而，募集AQP2的确切分子机制尚不清楚。最近的研究强调了肌动蛋白动力学的时空调节在AQP2转运中的关键作用。我们最近鉴定出了直接调节这种转运的AQP2结合蛋白：SPA-1，一种Rap1的GTP酶激活蛋白（GAP），以及细胞骨架蛋白肌动蛋白。此外，还发现了一种直接与AQP2结合的多蛋白“力发生器”复合物。本综述总结了与AQP2转运机制相关的最新进展。
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