Chemically induced dimerization: reversible and spatiotemporal control of protein function in cells

被引：112

作者：

Voss, Stephanie ^{[1
,2
]}

Klewer, Laura ^{[1
,2
]}

Wu, Yao-Wen ^{[1
,2
]}

机构：

[1] Max Planck Gesell, Chem Genom Ctr, D-44227 Dortmund, Germany

[2] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2015年 / 28卷

关键词：

SMALL GTPASE ACTIVITY; LIVING CELLS; SMALL-MOLECULE; ACTIVATION; SYSTEM; ASSAY; TRAFFICKING; PHENOTYPES; DISTINCT; KINASES;

D O I：

10.1016/j.cbpa.2015.09.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Small-molecule perturbation of biological systems is able to tackle biological problems that are not accessible by classical genetic interference methods. Chemically induced dimerization (CID) has been used as a valuable tool to study various biological processes. Recent years have seen tremendous progress in the development of orthogonal and reversible CID systems. These new systems allow control over protein function with unprecedented precision and spatiotemporal resolution. While the primary application of CID has been on dissecting signal transductions, new emerging approaches have extended the scope of this technique to elucidating membrane and protein trafficking.

引用

页码：194 / 201

页数：8

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