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首页> 外文期刊>Molecular biology of the cell >Characterization of the TPX2 domains involved in microtubule nucleation and spindle assembly in Xenopus egg extracts
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Characterization of the TPX2 domains involved in microtubule nucleation and spindle assembly in Xenopus egg extracts

机译：爪蟾卵提取物中涉及微管成核和纺锤体组装的TPX2结构域的表征

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摘要

TPX2 has multiple functions during mitosis, including microtubule nucleation around the chromosomes and the targeting of Xk1p2 and Aurora A to the spindle. We have performed a detailed domain functional analysis of TPX2 and found that a large N-terminal domain containing the Aurora A binding peptide interacts directly with and nucleates microtubules in pure tubulin solutions. However, it cannot substitute the endogenous TPX2 to support microtubule nucleation in response to Ran guanosine triphosphate (GTP) and spindle assembly in egg extracts. By contrast, a large C-terminal domain of TPX2 that does not bind directly to pure microtubules and does not bind Aurora A kinase rescues microtubule nucleation in response to RanGTP and spindle assembly in TPX2-depleted extract. These and previous results suggest that-under physiological conditions, TPX2 is essential for microtubule nucleation around chromatin and functions in a network of other molecules, some of which also are regulated by RanGTP.
机译：TPX2在有丝分裂过程中具有多种功能，包括染色体周围的微管成核以及Xk1p2和Aurora A靶向纺锤体。我们对TPX2进行了详细的域功能分析，发现包含Aurora A结合肽的N端大域与纯微管蛋白溶液中的微管直接相互作用并成核。但是，它不能替代内源性TPX2来支持卵磷脂提取物中的三磷酸鸟苷（GTP）和纺锤体装配，从而支持微管成核。相比之下，TPX2的大C末端结构域不直接结合纯微管，也不结合Aurora A激酶，可响应RanGTP和TPX2耗尽提取物中的纺锤体组装而拯救微管成核。这些和以前的结果表明，在生理条件下，TPX2对于染色质周围的微管成核是必不可少的，并在其他分子网络中起作用，其中一些也受RanGTP调节。

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