Macromolecular Structure and Function Laboratory, Cancer Research UK London Research Institute, London WC2A 3PX, England, UK.
J Cell Biol. 2010 Sep 6;190(5):823-34. doi: 10.1083/jcb.201002059.
The MIND multiprotein complex is a conserved, essential component of eukaryotic kinetochores and is a constituent of the tripartite KMN network that directly attaches the kinetochore to the mitotic spindle. The primary microtubule-binding complex in this network, NDC80, has been extensively characterized, but very little is known about the structure or function of the MIND complex. In this study, we present biochemical, hydrodynamic, electron microscopy, and small-angle x-ray scattering data that provide insight into the overall architecture and assembly of the MIND complex and the physical relationship of the complex with other components of the KMN network. We propose a model for the overall structure of the complex and provide data on the interactions with NDC80, Spc105p, and thus the mitotic spindle.
MIND 多蛋白复合物是真核动粒的保守、必需成分，也是直接将动粒连接到有丝分裂纺锤体的三部分 KMN 网络的组成部分。该网络中的主要微管结合复合物 NDC80 已得到广泛研究，但对 MIND 复合物的结构或功能知之甚少。在这项研究中，我们提供了生化、流体力学、电子显微镜和小角度 X 射线散射数据，这些数据深入了解了 MIND 复合物的整体结构和组装，以及复合物与 KMN 网络其他成分的物理关系。我们提出了该复合物的整体结构模型，并提供了与 NDC80、Spc105p 相互作用的数据，从而阐明了复合物与有丝分裂纺锤体的相互作用。
