The state of F-BAR domains as membrane-bound oligomeric platforms

被引:12
|
作者
Snider, Chloe E. [1 ]
Noor, Wan Nurul Izzati Wan Mohamad [2 ]
Nguyen, Nhung Thi Hong [2 ]
Gould, Kathleen L. [1 ]
Suetsugu, Shiro [2 ,3 ]
机构
[1] Vanderbilt Univ, Dept Cell & Dev Biol, Nashville, TN 37232 USA
[2] Nara Inst Sci & Technol, Div Biol Sci, 8916-5 Takayama, Nara 6300192, Japan
[3] Nara Inst Sci & Technol, Data Sci Ctr, 8916-5 Takayama, Nara 6300192, Japan
基金
美国国家卫生研究院; 日本学术振兴会; 日本科学技术振兴机构;
关键词
GTPASE-ACTIVATING PROTEIN; ACTIN CYTOSKELETON; RESOLUTION LIMIT; CELL-DIVISION; SH3; DOMAINS; BINDING; CDC15; TUBULATION; INVAGINATION; DEFORMATION;
D O I
10.1016/j.tcb.2021.03.013
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Fes/Cip4 homology Bin/amphiphysin/Rvs (F-BAR) domains, like all BAR domains, are dimeric units that oligomerize and bind membranes. F-BAR domains are generally coupled to additional domains that function in protein binding or have enzymatic activity. Because of their crescent shape and ability to oligomerize, F-BAR domains have been traditionally viewed as membrane-deformation modules. However, multiple independent studies have provided no evidence that certain F-BAR domains are able to tubulate membrane. Instead, a growing body of literature featuring structural, biochemical, biophysical, and microscopy-based studies supports the idea that the F-BAR domain family can be unified only by their ability to form oligomeric assemblies on membranes to provide platforms for molecular assembly.
引用
收藏
页码:644 / 655
页数:12
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