Engel A, Fujiyoshi Y, Agre P
M.E.Müller-Institute for Microscopy at the Biozentrum, University of Basel, CH-4056, Switzerland.
EMBO J. 2000 Mar 1;19(5):800-6. doi: 10.1093/emboj/19.5.800.
The history of the water channel and recent structural and functional analyses of aquaporins are reviewed. These ubiquitous channels are important for bacteria, plants and animals, exhibit a pronounced sequence homology and share functional as well as structural similarities. Aquaporins allow water or small specific solutes to pass unhindered, but block the passage of ions to prevent dissipation of the transmembrane potential. Besides advances in structure determination, recent experiments suggest that many of these channels are regulated by pH variations, phosphorylation and binding of auxiliary proteins.
本文综述了水通道的历史以及水通道蛋白最近的结构和功能分析。这些普遍存在的通道对细菌、植物和动物都很重要，它们表现出明显的序列同源性，并且在功能和结构上具有相似性。水通道蛋白允许水或特定的小分子溶质不受阻碍地通过，但会阻止离子通过，以防止跨膜电位的消散。除了在结构测定方面取得的进展外，最近的实验表明，许多这类通道受pH值变化、磷酸化和辅助蛋白结合的调节。
