Septin structure and function in yeast and beyond.

Septin structure and function in yeast and beyond.
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DOI:
10.1016/j.tcb.2010.11.006
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发表时间:
2011-03
影响因子:
19
通讯作者:
Bi E
Bi E
中科院分区:
生物学1区
文献类型:
--
作者:
Oh Y;Bi E

文献摘要

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间隔蛋白是一种保守的GTP结合蛋白,可以组装成异寡聚的复合体和更高阶的结构,如细丝、环、沙漏或纱布。Septins通常与质膜的一个离散区域相关联,作为细胞支架或扩散屏障来影响胞质分裂、细胞极性和许多其他细胞功能。最近对Septin复合体的结构研究已经为Septin细丝组装提供了机制方面的见解,但关于不同Septin细胞结构的组装、动力学和功能的关键问题在很大程度上仍未得到解答。
Septins are conserved GTP-binding proteins that assemble into hetero-oligomeric complexes and higher-order structures such as filaments, rings, hourglasses or gauzes. Septins are usually associated with a discrete region of the plasma membrane and function as a cellular scaffold or diffusion barrier to effect cytokinesis, cell polarity, and many other cellular functions. Recent structural studies of septin complexes have provided mechanistic insights into septin filament assembly, but key questions about the assembly, dynamics, and function of different septin cellular structures remain largely unanswered.