Dynein,一种古老的基于微管的运动蛋白,在几乎所有真核细胞中执行不同的细胞功能,除了陆地植物。它已经演变成三个亚家族-细胞质动力蛋白1,细胞质动力蛋白2和轴突动力蛋白-每个都通过其细胞功能而分化。这些巨型复合物由多个亚基组成,重链是最大的亚基,通过将ATP水解的化学能转化为机械功,沿着微管产生运动和力。除了这个催化核心,许多非催化亚基显着增强了动力蛋白的功能。这些亚基是复杂的组成部分,有助于其稳定,调节其酶活性,把它瞄准特定的细胞位置,并调解其与其他辅因子的相互作用。非催化亚基的多样性扩大了动力蛋白的细胞作用,使它能够执行关键任务,尽管它的重链被保护。在这次审查中,我们讨论了有关这些非催化亚基的最新发现和见解。
Dynein, an ancient microtubule-based motor protein, performs diverse cellular functions in nearly all eukaryotic cells, with the exception of land plants. It has evolved into three subfamilies-cytoplasmic dynein-1, cytoplasmic dynein-2, and axonemal dyneins-each differentiated by their cellular functions. These megadalton complexes consist of multiple subunits, with the heavy chain being the largest subunit that generates motion and force along microtubules by converting the chemical energy of ATP hydrolysis into mechanical work. Beyond this catalytic core, the functionality of dynein is significantly enhanced by numerous non-catalytic subunits. These subunits are integral to the complex, contributing to its stability, regulating its enzymatic activities, targeting it to specific cellular locations, and mediating its interactions with other cofactors. The diversity of non-catalytic subunits expands dynein\'s cellular roles, enabling it to perform critical tasks despite the conservation of its heavy chains. In this review, we discuss recent findings and insights regarding these non-catalytic subunits.