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Editorial
. 2018 Oct 18;10(10):2549-2550.
doi: 10.18632/aging.101605.

Identifying ubiquitinated proteins and aggregates

Nathan Basisty  1 , Birgit Schilling  1 , Peter S Rabinovitch  2
Affiliations
Editorial

Identifying ubiquitinated proteins and aggregates

Nathan Basisty et al. Aging (Albany NY). .
No abstract available

Keywords: aging; mass spectroscopy; protein aggregates; proteostasis; ubiquitination.

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Figures

Figure 1
Figure 1
Experimental design and workflow for predicting aggregating proteins in vivo in mice [2]. Following a treatment period, mice are metabolically labeled with 2H3-Leu over a specified timeframe (e.g. 17 days) to allow the calculation of protein turnover. Tissues are collected from mice in all experimental groups over multiple timepoints and processed into three fractions: ubiquitinated proteins, insoluble proteins, and soluble proteins. The ubiquitinated protein fraction is prepared via antibody enrichment. A multi-omic analysis that combines information about protein ubiquitination state, abundance in either the soluble or insoluble fractions, and turnover rate predicts proteins which are likely components of insoluble protein aggregates.
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References

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