Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells.

Epithelial cancers are often hallmarked by the overexpression of the Ser/Thr kinase Aurora A/AURKA. AURKA is a multifunctional protein that activates upon its autophosphorylation on Thr288. AURKA abundance peaks in mitosis, where it controls the stability and the fidelity of the mitotic spindle, and the overall efficiency of mitosis.

Automated screening of AURKA activity based on a genetically encoded FRET biosensor using fluorescence lifetime imaging microscopy.

Fluorescence Lifetime Imaging Microscopy (FLIM) is a robust tool to measure Förster Resonance Energy Transfer (FRET) between two fluorescent proteins, mainly when using genetically-encoded FRET biosensors. It is then possible to monitor biological processes such as kinase activity with a good spatiotemporal resolution and accuracy. Therefore, it is of interest to improve this methodology for future high content screening purposes.

Epsilon iron as a spin-smectic state.

Using X-ray emission spectroscopy, we find appreciable local magnetic moments until 30 GPa to 40 GPa in the high-pressure phase of iron; however, no magnetic order is detected with neutron powder diffraction down to 1.8 K, contrary to previous predictions. Our first-principles calculations reveal a "spin-smectic" state lower in energy than previous results.