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首页> 外文期刊>Cytoskeleton >Multiple domains of human CLASP contribute to microtubule dynamics and organization in vitro and in Xenopus egg extracts
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Multiple domains of human CLASP contribute to microtubule dynamics and organization in vitro and in Xenopus egg extracts

机译：人CLASP的多个域有助于体外和爪蟾卵提取物中的微管动力学和组织

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摘要

Cytoplasmic linker associated proteins (CLASPs) comprise a class of microtubule (MT) plus end-binding proteins (+TIPs) that contribute to the dynamics and organization of MTs during many cellular processes, among them mitosis. Human CLASP proteins contain multiple MT-binding domains, including tumor over-expressed gene (TOG) domains, and a Ser-x-Ile-Pro (SxIP) motif known to target some +TIPs though interaction with end-binding protein 1 (EB1). However, how individual domains contribute to CLASP function is poorly understood. We generated full-length recombinant human CLASP1 and a series of truncation mutants and found that two N-terminal TOG domains make the strongest contribution to MT polymerization and bundling, but also identified a third TOG domain that further contributes to CLASP activity. Plus end tracking by CLASP requires the SxIP motif and interaction with EB1. The C-terminal coiled-coil domain mediates dimerization and association with many other factors, including the kinetochore motor centromere protein E (CENP-E), and the chromokinesin Xkid. Only the full-length protein was able to rescue spindle assembly in Xenopus egg extracts depleted of endogenous CLASP. Deletion of the C-terminal domain caused aberrant MT polymerization and dramatic spindle phenotypes, even with small amounts of added protein, indicating that proper localization of CLASP activity is essential to control MT polymerization during mitosis.
机译：细胞质接头相关蛋白（CLASP）包括一类微管（MT）加上末端结合蛋白（+ TIP），它们在许多细胞过程（包括有丝分裂）中有助于MT的动力学和组织。人CLASP蛋白包含多个MT结合域，包括肿瘤过度表达的基因（TOG）域和一个Ser-x-Ile-Pro（SxIP）模体，该基序通过与末端结合蛋白1（EB1）相互作用而靶向某些+ TIP ）。但是，人们对单个域如何促进CLASP功能的了解很少。我们生成了全长重组人CLASP1和一系列截短突变体，发现两个N末端TOG域对MT聚合和成束作用最强，但还确定了第三个TOG结构域，进一步促进CLASP活性。再加上CLASP的末端跟踪，需要SxIP图案并与EB1相互作用。 C末端的卷曲螺旋结构域介导二聚化并与许多其他因素相关联，包括动粒体运动着丝粒蛋白E（CENP-E）和色激酶Xkid。只有全长蛋白才能挽救耗尽内源性CLASP的非洲爪蟾卵提取物中的纺锤体组装。 C-末端结构域的缺失导致异常的MT聚合和剧烈的纺锤表型，即使添加少量蛋白质也是如此，这表明CLASP活性的适当定位对于控制有丝分裂期间的MT聚合至关重要。

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