Institut für Organische und Biomolekulare Chemie, Georg-August Universität, Tammannstr. 2, 37077 Göttingen, Germany.
Biophys Chem. 2010 Aug;150(1-3):47-53. doi: 10.1016/j.bpc.2010.02.005. Epub 2010 Feb 11.
The pkd1 and pkd2 genes encode for the proteins polycystin-1 (PC1) and polycystin-2 (PC2). These genes are mutated in patients diagnosed with autosomal dominant polycystic kidney disease. PC1 and PC2 interact via their C-terminal, cytosolic regions, which is an essential step in the regulation of cell proliferation and differentiation. Here, we developed an assay that allowed us to quantitatively monitor the interaction of the C-terminal region of PC1 (cPC1) with that of PC2 (cPC2) to be able to answer the question of how Ca(2+) influences the PC1/PC2 complex formation. By means of the quartz crystal microbalance (QCM) technique, we were able to determine binding affinities and kinetic constants of the cPC1/cPC2 interaction using a model based on the scaled particle theory. The results suggest that cPC2 forms trimers in solution in the absence of Ca(2+), which bind in a one step process to cPC1.
pkd1 和 pkd2 基因分别编码多囊蛋白-1（PC1）和多囊蛋白-2（PC2）。这些基因的突变会导致常染色体显性多囊肾病。PC1 和 PC2 通过它们的 C 端胞质区域相互作用，这是调节细胞增殖和分化的关键步骤。在这里，我们开发了一种可以定量监测 PC1 的 C 端区域（cPC1）与 PC2（cPC2）相互作用的检测方法，以便回答 Ca（2+）如何影响 PC1/PC2 复合物形成的问题。我们使用基于比例粒子理论的模型，通过石英晶体微天平（QCM）技术，确定了 cPC1/cPC2 相互作用的结合亲和力和动力学常数。结果表明，cPC2 在没有 Ca（2+）的情况下在溶液中形成三聚体，它们以一步过程与 cPC1 结合。
