Key Laboratory of Soft Matter Physics , Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Int J Biol Sci. 2010 Nov 3;6(7):665-74. doi: 10.7150/ijbs.6.665.
Kinesin molecules are motor proteins capable of moving along microtubule by hydrolyzing ATP. They generally have several forms of construct. This review focuses on two of the most studied forms: monomers such as KIF1A (kinesin-3 family) and dimers such as conventional kinesin (kinesin-1 family), both of which can move processively towards the microtubule plus end. There now exist numerous models that try to explain how the kinesin molecules convert the chemical energy of ATP hydrolysis into the mechanical energy to "power" their processive movement along microtubule. Here, we attempt to present a comprehensive review of these models. We further propose a new hybrid model for the dimeric kinesin by combining the existing models and provide a framework for future studies in this subject.
驱动蛋白分子是能够通过水解 ATP 沿微管运动的马达蛋白。它们通常有几种形式的结构。本综述重点介绍两种研究最多的形式：单体，如 KIF1A（驱动蛋白-3 家族）和二聚体，如传统驱动蛋白（驱动蛋白-1 家族），它们都可以向微管正端进行连续运动。现在有许多模型试图解释驱动蛋白分子如何将 ATP 水解的化学能转化为机械能，以“驱动”它们沿着微管的连续运动。在这里，我们试图对这些模型进行全面的综述。我们进一步通过结合现有模型，为二聚体驱动蛋白提出了一个新的混合模型，并为该领域的未来研究提供了一个框架。
