Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 11, Pages 3338-3343Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1502857112
Keywords
protease; fluorogenic reporters; bacterial phytochrome; apoptosis; tumor development
Categories
Funding
- University of California, San Francisco start-up funds
- Howard Hughes Medical Institute
- National Institutes of Health
- Lefkofsky Family-Damon Runyon Fellowship [DRG:2161-13]
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Fluorescence resonance energy transfer-based reporters have been widely used in imaging cell signaling; however, their in vivo application has been handicapped because of poor signal. Although fluorogenic reporters overcome this problem, no such reporter of proteases has been demonstrated for in vivo imaging. Now we have redesigned an infrared fluorescent protein so that its chromophore incorporation is regulated by protease activity. Upon protease activation, the infrared fluorogenic protease reporter becomes fluorescent with no requirement of exogenous cofactor. To demonstrate biological applications, we have designed an infrared fluorogenic executioner-caspase reporter, which reveals spatiotemporal coordination between cell apoptosis and embryonic morphogenesis, as well as dynamics of apoptosis during tumorigenesis in Drosophila. The designed scaffold may be used to engineer reporters of other proteases with specific cleavage sequence.
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