Live-cell quantitative imaging of proteome degradation by stimulated Raman scattering
- Creators
- Shen, Yihui
- Xu, Fang
- Wei, Lu
- Hu, Fanghao
- Min, Wei
Abstract
Protein degradation is a regulatory process essential to cell viability and its dysfunction is implicated in many diseases, such as aging and neurodegeneration. In this report, stimulated Raman scattering microscopy coupled with metabolic labeling with ^(13)C-phenylalanine is used to visualize protein degradation in living cells with subcellular resolution. We choose the ring breathing modes of endogenous ^(12)C-phenylalanine and incorporated ^(13)C-phenylalanine as protein markers for the original and nascent proteomes, respectively, and the decay of the former wasquantified through ^(12)C/(^(12)C + ^(13)C) ratio maps. We demonstrate time-dependent imaging of proteomic degradation in mammalian cells under steady-state conditions and various perturbations, including oxidative stress, cell differentiation, and huntingtin protein aggregation.
Additional Information
© 2014 WILEY‐VCH. Received: December 10, 2013. Published online: April 15, 2014. W.M. acknowledges support from National Institutes of Health Director's New Innovator Award and Sloan Research Fellowship.Attached Files
Accepted Version - nihms597333.pdf
Supplemental Material - anie_201310725_sm_miscellaneous_information.pdf
Files
Name | Size | Download all |
---|---|---|
md5:d1defa6106096a897107bb8c5053154d
|
2.8 MB | Preview Download |
md5:a561c1f1c117bcce193ab9f1c4b16e54
|
772.8 kB | Preview Download |
Additional details
- PMCID
- PMC4231775
- Eprint ID
- 86927
- DOI
- 10.1002/anie.201310725
- Resolver ID
- CaltechAUTHORS:20180608-133129304
- NIH
- Alfred P. Sloan Foundation
- Created
-
2018-06-08Created from EPrint's datestamp field
- Updated
-
2021-11-15Created from EPrint's last_modified field