Protein degradation is essential to maintain proteostasis in cells, and dysfunction of protein degradation systems results in numerous diseases. Despite the importance of protein degradation, the degradation pathways of many proteins remain to be explored. Here, we comprehensively investigated the degradation of newly synthesized proteins in human cells by integrating metabolic labeling, click chemistry, and multiplexed proteomics. This systematic and quantitative analysis revealed the degradation pathways of many proteins. Bioinformatics analysis demonstrated that proteins degraded through two major pathways had distinct properties and functions. Proteins degraded through the proteasome contained more disordered structures, whereas those through the lysosome pathway had significantly higher hydrophobicity. In addition, we studied proteins in the proteasome and ribosome complexes and in the glycolysis and endocytosis pathways. Systematic investigation of the dynamics of newly synthesized proteins provides valuable information about protein degradation, which leads to a better understanding of protein properties and cellular activities.

Systematic quantification of the dynamics of newly synthesized proteins in human cells unveiling their degradation pathways

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.