微管相关蛋白tau对长春花碱诱导的微管蛋白聚集的影响。
Effect of tau on the vinblastine-induced aggregation of tubulin.
作者信息
Ludueña R F, Fellous A, Francon J, Nunez J, McManus L
出版信息
J Cell Biol. 1981 Jun;89(3):680-3. doi: 10.1083/jcb.89.3.680.
Abstract
Two microtubule-associated proteins, tau and the high molecular weight microtubule-associated protein 2 (MAP 2), were purified from rat brain microtubules. Addition of either protein to pure tubulin caused microtubule assembly. In the presence of tau and 10 microM vinblastine, tubulin aggregated into spiral structures. If tau was absent, or replaced by MAP 2, little aggregation occurred in the presence of vinblastine. Thus, vinblastine may be a useful probe in elucidating the individual roles of tau and MAP 2 in microtubule assembly.
摘要
从大鼠脑微管中纯化出两种微管相关蛋白，即tau蛋白和高分子量微管相关蛋白2（MAP 2）。将这两种蛋白中的任何一种添加到纯微管蛋白中都会导致微管组装。在tau蛋白和10微摩尔长春花碱存在的情况下，微管蛋白聚集成螺旋结构。如果没有tau蛋白，或者用MAP 2替代，在长春花碱存在的情况下几乎不会发生聚集。因此，长春花碱可能是阐明tau蛋白和MAP 2在微管组装中各自作用的有用探针。
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