Getting to the heart of beta-tubulin
Getting to the heart of beta-tubulin
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DOI：
10.1016/0962-8924(96)10024-6
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发表时间：
1996-08-01
影响因子：
19
通讯作者：
Farrell, KW
中科院分区：
文献类型：
--
作者：
Burns, RG;Farrell, KW
细胞微管以不同的速率和频率组装和分解，这些特性直接有助于细胞周期相关的微管细胞骨架的重排和有丝分裂的分子基础。装配/拆卸的动力学部分受结合到β-微管蛋白核苷酸结合位点的GTP的水解所支配。因此，β-微管蛋白GTP结合位点位于微管组装-拆解动力学的核心，其结构的阐明对于理解微管的细胞行为至关重要。不幸的是，β-微管蛋白的晶体结构尚不清楚。在这篇综述中，我们描述了利用突变和生化研究来了解这个不寻常的GTP结合位点的结构所取得的进展。
Cellular microtubules assemble and disassemble at a variety of rates and frequencies, and these properties contribute directly to the cell-cycle-associated rearrangements of the microtubule cytoskeleton and to the molecular basis of mitosis. The kinetics of assembly/disassembly are governed, in part, by the hydrolysis of GTP bound to the beta-tubulin nucleotide-binding site. The beta-tubulin GTP-binding site, therefore, lies at the heart of microtubule assembly-disassembly kinetics, and the elucidation of its structure is central to an understanding of the cellular behaviour of microtubules. Unfortunately, the crystallographic structure of beta-tubulin is not yet available. In this review, we describe the progress being made using mutagenesis and biochemical studies to understand the structure of this unusual GTP-binding site.