Chui K K, Rogers G C, Kashina A M, Wedaman K P, Sharp D J, Nguyen D T, Wilt F, Scholey J M
Section of Molecular and Cellular Biology, University of California, Davis, California 95616, USA.
J Biol Chem. 2000 Dec 1;275(48):38005-11. doi: 10.1074/jbc.M005948200.
To improve our understanding of the roles of microtubule cross-linking motors in mitosis, we analyzed two sea urchin embryonic kinesin-related proteins. It is striking to note that both of these proteins behave as homotetramers, but one behaves as a more compact molecule than the other. These observations suggest that these two presumptive motors could cross-link microtubules into bundles with different spacing. Both motors localize to mitotic spindles, and antibody microinjection experiments suggest that they have mitotic functions. Thus, one of these kinesin-related proteins may cross-link spindle microtubules into loose bundles that are "tightened" by the other.
为了增进我们对微管交联马达蛋白在有丝分裂中作用的理解,我们分析了两种海胆胚胎中与驱动蛋白相关的蛋白。值得注意的是,这两种蛋白均表现为同四聚体,但其中一种比另一种表现为更紧密的分子。这些观察结果表明,这两种假定的马达蛋白可能将微管交联成具有不同间距的束状结构。两种马达蛋白均定位于有丝分裂纺锤体,并且抗体显微注射实验表明它们具有有丝分裂功能。因此,这些与驱动蛋白相关的蛋白之一可能将纺锤体微管交联成松散的束状结构,而另一种则使其“收紧”。