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首页> 外文期刊>Molecular biology of the cell >Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
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Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.

机译：微管相关蛋白tau对微管蛋白装配动态不稳定性的调节。

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摘要

Microtubule-associated proteins (MAP), such as tau, modulate the extent and rate of microtubule assembly and play an essential role in morphogenetic processes, such as axonal growth. We have examined the mechanism by which tau affects microtubule polymerization by examining the kinetics of microtubule assembly and disassembly through direct observation of microtubules using dark-field microscopy. Tau increases the rate of polymerization, decreases the rate of transit into the shrinking phase (catastrophe), and inhibits the rate of depolymerization. Tau strongly suppresses the catastrophe rate, and its ability to do so is independent of its ability to increase the elongation rate. Thus, tau generates a partially stable but still dynamic state in microtubules. This state is perturbed by phosphorylation by MAP2 kinase, which affects all three activities by lowering the affinity of tau for the microtubule lattice.
机译：微管相关蛋白（MAP），例如tau，可调节微管组装的程度和速率，并在形态发生过程（如轴突生长）中起重要作用。我们通过使用暗场显微镜直接观察微管，检查微管组装和拆卸的动力学，从而研究了tau影响微管聚合的机制。 Tau提高了聚合速率，降低了进入收缩相的转变速率（灾难性），并抑制了解聚速率。 Tau强烈地抑制了突变率，并且其抑制能力与增加伸长率的能力无关。因此，tau在微管中产生了部分稳定但仍处于动态状态。这种状态会受到MAP2激酶的磷酸化作用的干扰，而MAP2激酶通过降低tau对微管晶格的亲和力来影响所有三种活性。

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