Kinesin-13s form rings around microtubules.
Kinesin-13s form rings around microtubules.
复制标题
动力蛋白13S周围形成环。
DOI：
10.1083/jcb.200605194
复制
发表时间：
2006-10-09
影响因子：
7.8
通讯作者：
Sosa, Hernando
中科院分区：
文献类型：
--
作者：
Tan, Dongyan;Asenjo, Ana B;Mennella, Vito;Sharp, David J;Sosa, Hernando
动蛋白是一个超家族的马达蛋白，它利用三磷酸腺苷的水解能量沿微管移动并产生力量。这一一般性描述的一个明显的例外是在Kinesin-13家族中发现的，该家族主动解聚微管而不是主动沿微管移动。这种解聚活性在染色体分离期间的有丝分裂中是重要的。目前尚不完全清楚Kinesin-13S解聚微管的机制。为了解决这个问题，我们使用电子显微镜来研究kinesin-13s与微管的相互作用。令人惊讶的是，我们发现Kinesin-13家族的蛋白质在微管周围形成环状和螺旋状。这是首次报道任何激动素蛋白的这种类型的寡聚体结构。这些环可能允许Kinesin-13在解聚过程中停留在微管的末端。
Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving along them. This depolymerization activity is important in mitosis during chromosome segregation. It is still not fully clear by which mechanism kinesin-13s depolymerize microtubules. To address this issue, we used electron microscopy to investigate the interaction of kinesin-13s with microtubules. Surprisingly, we found that proteins of the kinesin-13 family form rings and spirals around microtubules. This is the first report of this type of oligomeric structure for any kinesin protein. These rings may allow kinesin-13s to stay at the ends of microtubules during depolymerization.