bioRxivJClub
N-terminal cysteine independent effects of oxidative stress on the stability of RGS4 and 5
bioRxiv · · Preprint · Open access
Kim, Shang + 3 more
Abstract ↗AI summary
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Cytotoxic tert-butyl hydroperoxide increases RGS4/5 protein stability substantially, independently of the Cys N-degron pathway, and this stabilization is blocked by Fe2+ chelation, lysosomal pH perturbation, and lipid peroxide scavenging.
- Why it matters: It remains unclear whether N-terminal cysteine dioxygenation depends on ADO under oxidative conditions, and whether oxidative stress alters RGS4/5 stability via the Cys N-degron pathway.
- What they did: The study used a cellular system that generates titratable intracellular H2O2 levels to test RGS4 and RGS5 stability with or without ADO, then challenged cells with tert-butyl hydroperoxide.
- The result: Physiological oxidative stress does not affect RGS4/5 stability regardless of ADO, but oxidative stress-induced cell death stabilizes these proteins via an N-terminal cysteine independent mechanism.
The findingWhy it mattersWhat they didThe result
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