The role of microtubule assembly dynamics in mitotic force generation and functional organization of living cells

The role of microtubule assembly dynamics in mitotic force generation and functional organization of living cells
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DOI:
10.1006/jsbi.1996.3839
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发表时间:
1997-03-01
影响因子:
3
通讯作者:
Inoue, S
Inoue, S
中科院分区:
生物学3区
文献类型:
--
作者:
Inoue, S

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本文总结了作者在 1996 年 4 月 12 日至 14 日在德克萨斯州休斯敦举行的贝勒医学院微管生物物理学研讨会上的演讲。它提供了一个简短的历史概述,并讨论了微管的组装/拆卸可能在活细胞中染色体运动和相关细胞器定位的力产生中发挥的作用。这篇文章首先介绍了活细胞的偏光显微镜如何在 20 世纪 50 年代和 1960 年代为这一概念奠定了基础,但在发现由 ATP 水解运动蛋白动力蛋白驱动的微管滑动产生力后,该概念在接下来的 20 年里黯然失色。最近有趣的发现:微管经历动态不稳定;它们都在附着于染色体的动粒处组装和分解;即使在没有可水解核苷酸的情况下,组装和拆卸微管本身也可以在模型实验中推拉合理的负载,这使得人们重新将注意力集中在微管组装/拆卸可能发挥的作用上。这种力产生模式很可能与“运动”蛋白质所发挥的力产生和/或动态附着作用(尤其是在动粒处)错综复杂地耦合和相互作用。 (C) 1997 年学术出版社。
This article summarizes the author's presentation at the Baylor Medical School Symposium on the Biophysics of Microtubules, held April 12 to 14, 1996, in Houston, Texas. It presents a brief historical sketch and discusses the role that assembly/disassembly of microtubules is likely to be playing in force generation for chromosome movement and related organellar positioning in living cells. The article starts out with how polarized light microscopy of living cells had laid the foundation for this concept in the 1950s and 1960s, but was then eclipsed for some 2 decades following the discovery of force generation by microtubule sliding powered by an ATP-hydrolyzing motor protein, dynein. The intriguing recent discoveries: that microtubules undergo dynamic instability; that they both assemble and disassemble right at the kinetochore where they are attached to the chromsome; and that assembling and disassembling microtubules can of themselves push and pull reasonable loads in model experiments, even in the absence of hydrolyzable nucleotides, have refocused serious attention on the probable role played by assembly/disassembly of microtubules. This mode of force generation may well be intricately coupled, and interact, with force-generating and/or dynamic attachment roles played by ''motor'' proteins, especially at the kinetochore. (C) 1997 Academic Press.