1932

Abstract

Abstract

Signaling pathways regulating proliferation, differentiation, and inflammation are commonly mediated through protein-protein interactions as well as reversible modification (e.g., phosphorylation) of proteins. To facilitate the study of regulated protein-protein interactions in cells and living animals, new imaging tools, many based on optical signals and capable of quantifying protein interactions in vivo, have advanced the study of induced protein interactions and their modification, as well as accelerated the rate of acquisition of these data. In particular, use of protein fragment complementation as a reporter strategy can accurately and rapidly dissect protein interactions with a variety of readouts, including absorbance, fluorescence, and bioluminescence. This review focuses on the development and validation of bioluminescent protein fragment complementation reporters that use either luciferase or firefly luciferase in vivo. Enhanced luciferase complementation provides a platform for near real-time detection and characterization of regulated and small-molecule-induced protein-protein interactions in intact cells and living animals and enables a wide range of novel applications in drug discovery, chemical genetics, and proteomics research.

Loading

Article metrics loading...

/content/journals/10.1146/annurev.bioeng.9.060906.152044
2007-08-15
2024-06-14
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.bioeng.9.060906.152044
Loading
/content/journals/10.1146/annurev.bioeng.9.060906.152044
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error