Filling the Void: Proximity-Based Labeling of Proteins in Living Cells

被引:115
作者
Kim, Dae In [1 ]
Roux, Kyle J. [1 ,2 ]
机构
[1] Sanford Res, Sanford Childrens Hlth Res Ctr, Sioux Falls, SD 57104 USA
[2] Univ South Dakota, Sanford Sch Med, Dept Pediat, Sioux Falls, SD 57105 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
ENGINEERED ASCORBATE PEROXIDASE; ENZYME-MEDIATED ACTIVATION; PROTEOMIC ANALYSIS; BIOTIN LIGASE; HORSERADISH-PEROXIDASE; INTERACTING PARTNERS; AMINO-ACID; E-CADHERIN; BIOTINYLATION; MEMBRANE;
D O I
10.1016/j.tcb.2016.09.004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
There are inherent limitations with traditional methods to study protein behavior or to determine the constituency of proteins in discrete subcellular compartments. In response to these limitations, several methods have recently been developed that use proximity-dependent labeling. By fusing proteins to enzymes that generate reactive molecules, most commonly biotin, proximate proteins are covalently labeled to enable their isolation and identification. In this review we describe current methods for proximity-dependent labeling in living cells and discuss their applications and future use in the study of protein behavior.
引用
收藏
页码:804 / 817
页数:14
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