Septin structure and function in yeast and beyond

被引：169

作者：

Oh, Younghoon ^{[1
]}

Bi, Erfei ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA

来源：

TRENDS IN CELL BIOLOGY | 2011年 / 21卷 / 03期

基金：

美国国家卫生研究院;

关键词：

SPERM TERMINAL DIFFERENTIATION; GTPASE-ACTIVATING PROTEINS; BUDDING YEAST; SACCHAROMYCES-CEREVISIAE; CELL-CYCLE; MAMMALIAN SEPTINS; FISSION YEAST; DIRECT PHOSPHORYLATION; NUCLEOTIDE-BINDING; FILAMENT FORMATION;

D O I：

10.1016/j.tcb.2010.11.006

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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 cell scaffold or diffusion barrier to effect cytokinesis, cell polarity, and many other functions. Recent structural studies of septin complexes have provided mechanistic insights into septin filament assembly, but key questions concerning the assembly, dynamics, and function of different septin structures remain to be answered.

引用

页码：141 / 148

页数：8

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