Quantifying protein dynamics and stability in a living organism

As an integral part of modern cell biology, fluorescence microscopy enables quantification of the stability and dynamics of fluorescence-labeled biomolecules inside cultured cells. However, obtaining time-resolved data from individual cells within a live vertebrate organism remains challenging. Here we demonstrate a customized pipeline that integrates meganuclease-mediated mosaic transformation with fluorescence-detected temperaturejump microscopy to probe dynamics and stability of endogenously expressed proteins in different tissues of living multicellular organisms.