Quantifying protein dynamics and stability in a living organism.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30862837.
- Also identified by DOI 10.1038/s41467-019-09088-y and PMC identifier 6414637.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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 temperature-jump microscopy to probe dynamics and stability of endogenously expressed proteins in different tissues of living multicellular organisms.
Medical subject headings
- Fungal Proteins
- Intravital Microscopy
- Phosphoglycerate Kinase