Cellular protein homeostasis entails regulating protein production, location, and degradation primarily through the ubiquitin-proteasome system. This process relies on specific post-translational modifications (PTMs) like poly-ubiquitylation. Despite extensive knowledge about PTMs, the impact of non-enzymatic modifications on protein stability and degradation mechanisms is less understood. This study focuses on C-terminal amides as potential degrons while employing semi-synthetic fluorescent reporters to observe how different chemical modifications affect protein turnover in human cells. The findings may offer insights into degradation mechanisms linked to unexplored protein modifications, enhancing the understanding of cellular protein management.
The ubiquitin-proteasome system plays a critical role in cellular protein homeostasis by selectively degrading proteins, with over 600 human ubiquitin ligases regulating this process.
Non-canonical post-translational modifications, including oxidative damage, impact protein turnover, yet the specific mechanisms of their recognition for degradation remain largely unexplored.
Our study employs a reductionist approach to investigate the influence of specific chemical modifications on protein turnover, using semi-synthetic fluorescent reporters in human cells.
C-terminal amides have been identified as functionally significant degrons, marking proteins for degradation and highlighting the complexity of post-translational modifications in protein homeostasis.
#protein-degradation #ubiquitin-proteasome-system #post-translational-modifications #cellular-biology #proteostasis
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