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Monthly Archives: March 2013
The study of cell signaling has revealed that cells can be particularly sensitive to spatiotemporal properties of the signaling dynamics. For instance, a cell can choose divergent fates (proliferation vs. differentiation, senescence vs. apoptosis, etc.) depending on the duration and strength of a protein signal. The development of fluorescent reporters has enabled us to observe these dynamics, but researchers still lack appropriate, general tools to perturb cells on the second- and minute-timescales on which signaling dynamics can occur.
Coupling light to protein activation may offer a powerful solution due to its fast, reversible, and highly tunable nature. In the March 2013 issue of Nature Methods, Bugaj, Kane, Schaffer and colleagues accomplish this by developing a method for light inducible homo-oligomerization of proteins. In this study, the authors report a genetically encodable, generalizable system that can activate multiple signaling proteins and networks in mammalian cells.
To do this, the authors leveraged the interesting ability of the Arabidopsis protein Cryptochrome 2 (Cry2) to form oligomers in response to blue light. To date, this clustering ability had only been shown in plant cells, but upon transfection into HEK 293Ts, the authors demonstrated that Cry2 can be clustered in mammalian cells as well (fig. … Continue reading