Buzhynskyy Nikolay, Hite Richard K, Walz Thomas, Scheuring Simon
Institut Curie, UMR168-CNRS, 26 Rue d'Ulm, 75248 Paris, France.
EMBO Rep. 2007 Jan;8(1):51-5. doi: 10.1038/sj.embor.7400858. Epub 2006 Nov 24.
Gap junctions formed by connexons and thin junctions formed by lens-specific aquaporin 0 (AQP0) mediate the tight packing of fibre cells necessary for lens transparency. Gap junctions conduct water, ions and metabolites between cells, whereas junctional AQP0 seems to be involved in cell adhesion. High-resolution atomic force microscopy (AFM) showed the supramolecular organization of these proteins in native lens core membranes, in which AQP0 forms two-dimensional arrays that are surrounded by densely packed gap junction channels. These junctional microdomains simultaneously provide adhesion and communication between fibre cells. The AFM topographs also showed that the extracellular loops of AQP0 in junctional microdomains adopt a conformation that closely resembles the structure of junctional AQP0, in which the water pore is thought to be closed. Finally, time-lapse AFM imaging provided insights into AQP0 array formation. This first high-resolution view of a multicomponent eukaryotic membrane shows how membrane proteins self-assemble into functional microdomains.
由连接子形成的间隙连接以及由晶状体特异性水通道蛋白0(AQP0)形成的紧密连接介导了晶状体纤维细胞紧密排列,这对晶状体透明性至关重要。间隙连接在细胞间传导水、离子和代谢物,而连接性AQP0似乎参与细胞黏附。高分辨率原子力显微镜(AFM)显示了这些蛋白质在天然晶状体核心膜中的超分子组织,其中AQP0形成二维阵列,被密集排列的间隙连接通道包围。这些连接微结构域同时提供纤维细胞之间的黏附和通讯。AFM地形图还显示,连接微结构域中AQP0的细胞外环采用的构象与连接性AQP0的结构非常相似,其中水孔被认为是关闭的。最后,延时AFM成像为AQP0阵列形成提供了见解。这种对多组分真核细胞膜的首次高分辨率观察展示了膜蛋白如何自组装成功能性微结构域。