期刊
ACS CHEMICAL BIOLOGY
卷 16, 期 11, 页码 2434-2443出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.1c00547
关键词
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资金
- National Science Foundation [CHE-1404836]
- National Science Foundation
A new caged rapamycin analog has been developed with minimal background activity for protein dimerization and easy integration with established FKBP/FRB systems. It has been successfully used for optical control of protein function and signaling pathways.
Rapamycin-induced dimerization of FKBP and FRB is the most commonly utilized chemically induced protein dimerization system. It has been extensively used to conditionally control protein localization, split-enzyme activity, and protein-protein interactions in general by simply fusing FKBP and FRB to proteins of interest. We have developed a new aminonitrobiphenylethyl caging group and applied it to the generation of a caged rapamycin analog that can be photoactivated using blue light. Importantly, the caged rapamycin analog shows minimal background activity with regard to protein dimerization and can be directly interfaced with a wide range of established (and often commercially available) FKBP/FRB systems. We have successfully demonstrated its applicability to the optical control of enzymatic function, protein stability, and protein subcellular localization. Further, we also showcased its applicability toward optical regulation of cell signaling, specifically mTOR signaling, in cells and aquatic embryos.
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