Tau protein binds to microtubules through a flexible array of distributed weak sites.

Tau protein binds to microtubules through a flexible array of distributed weak sites.
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DOI:
10.1083/jcb.115.3.717
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发表时间:
1991-11
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Kirschner MW
Kirschner MW
中科院分区:
其他
文献类型:
--
作者:
Butner KA;Kirschner MW

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Tau蛋白通过与微管的直接关联在神经元过程的延伸和维持中起作用。为了表征这种关联的性质,我们合成了一系列tau蛋白片段,并研究了它们的结合特性。tau蛋白对微管的亲和力相对较弱(约10(-7)M),主要集中在一个含有3个或4个18个氨基酸重复结合元件的大区域。它们被不结合的13-14个氨基酸的明显柔性但不太保守的接头序列分开。在重复序列内,微管的结合能是离域的,并且来自于由小的氨基酸基团贡献的一系列弱相互作用。这些不寻常的特征表明tau蛋白可以呈现多种构象,并且可以在微管表面上枢转并可能迁移。tau蛋白结合相互作用的灵活结构可以使其容易地从微管晶格中置换,并且可能对其功能具有重要影响。
Tau protein plays a role in the extension and maintenance of neuronal processes through a direct association with microtubules. To characterize the nature of this association, we have synthesized a collection of tau protein fragments and studied their binding properties. The relatively weak affinity of tau protein for microtubules (approximately 10(-7) M) is concentrated in a large region containing three or four 18 amino acid repeated binding elements. These are separated by apparently flexible but less conserved linker sequences of 13-14 amino acids that do not bind. Within the repeats, the binding energy for microtubules is delocalized and derives from a series of weak interactions contributed by small groups of amino acids. These unusual characteristics suggest tau protein can assume multiple conformations and can pivot and perhaps migrate on the surface of the microtubule. The flexible structure of the tau protein binding interaction may allow it to be easily displaced from the microtubule lattice and may have important consequences for its function.
DOI: 10.1083/jcb.107.4.1449
发表时间: 1988-10
期刊: The Journal of cell biology
影响因子: --
作者:
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期刊: The Journal of cell biology
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