The Aspergillus nidulans Kinesin-3 Tail Is Necessary and Sufficient to Recognize Modified Microtubules

The Aspergillus nidulans Kinesin-3 Tail Is Necessary and Sufficient to Recognize Modified Microtubules
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构巢曲霉驱动蛋白 3 尾对于识别修饰的微管是必要且充分的

DOI:
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
R. Fischer
R. Fischer
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Constanze Seidel;Nadine Zekert;R. Fischer

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翻译后微管修饰(PTMs)是众多的,然而,这些修饰的生物化学和细胞生物学作用仍然是一个谜。构巢曲霉驱动蛋白-3UncA优选使用修饰的微管(MT)作为囊泡运输的轨道。在这里,我们表明,带正电荷的区域在尾部的UncA(氨基酸1316至1402)是必要的识别修饰的MT。由驱动蛋白-1马达结构域和UncA尾组成的嵌合蛋白显示出与UncA相同的特异性,表明UncA尾足以建立特异性。使用酵母双杂交测定和A.通过双分子荧光互补作用对nidulans进行修饰。这是第一次证明驱动蛋白-3马达蛋白如何区分真菌细胞中不同的MT群体,以及特异性决定如何取决于尾部而不是马达结构域,如神经元细胞中驱动蛋白1所示。
Posttranslational microtubule modifications (PTMs) are numerous; however, the biochemical and cell biological roles of those modifications remain mostly an enigma. The Aspergillus nidulans kinesin-3 UncA uses preferably modified microtubules (MTs) as tracks for vesicle transportation. Here, we show that a positively charged region in the tail of UncA (amino acids 1316 to 1402) is necessary for the recognition of modified MTs. Chimeric proteins composed of the kinesin-1 motor domain and the UncA tail displayed the same specificity as UncA, suggesting that the UncA tail is sufficient to establish specificity. Interaction between the UncA tail and alpha-tubulin was shown using a yeast two-hybrid assay and in A. nidulans by bimolecular fluorescence complementation. This is the first demonstration of how a kinesin-3 motor protein distinguishes among different MT populations in fungal cells, and how specificity determination depends on the tail rather than the motor domain, as has been demonstrated for kinesin 1 in neuronal cells.
DOI: 10.1073/pnas.81.5.1470
发表时间: 1984-01-01
期刊: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子: --
作者:
YELTON, MM;HAMER, JE;TIMBERLAKE, WE
通讯作者: TIMBERLAKE, WE
DOI: 10.1002/cm.20392
发表时间: 2009-11
影响因子: --
作者:
Marx, Alexander;Hoenger, Andreas;Mandelkow, Eckhard
通讯作者: Mandelkow, Eckhard