Department of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
FEBS Lett. 2013 Jun 5;587(11):1587-91. doi: 10.1016/j.febslet.2013.04.006. Epub 2013 Apr 18.
The axis inhibition (Axin) scaffold protein colocalizes β-catenin, casein kinase Iα, and glycogen synthetase kinase 3β by their binding to Axin's long intrinsically disordered region, thereby yielding structured domains with flexible linkers. This complex leads to the phosphorylation of β-catenin, marking it for destruction. Fusing proteins with flexible linkers vastly accelerates chemical interactions between them by their colocalization. Here we propose that the complex works by random movements of a "stochastic machine," not by coordinated conformational changes. This non-covalent, modular assembly process allows the various molecular machine components to be used in multiple processes.
轴抑制（Axin）支架蛋白通过与其长的固有无序区域结合，使β-catenin、酪蛋白激酶 Iα 和糖原合成酶激酶 3β 共定位，从而产生具有柔性接头的结构域。该复合物导致β-catenin 的磷酸化，标记其进行破坏。通过共定位，将具有柔性接头的蛋白质融合可大大加速它们之间的化学相互作用。在这里，我们提出该复合物通过“随机机器”的随机运动而不是协调的构象变化来工作。这种非共价的、模块化的组装过程允许各种分子机器组件在多个过程中使用。
