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iRQC, a surveillance pathway for 40S ribosomal quality control during mRNA translation initiation

Cell Rep. 2021-08; 
Danielle M Garshott, Heeseon An, Elayanambi Sundaramoorthy, Marilyn Leonard, Alison Vicary, J Wade Harper, Eric J Bennett
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Proteins, Expression, Isolation and Analysis  Following elution, 100U of His-TEV protease (Z03030-1K, GenScript) was added to the 1:1 slurry of resin in elution buffer and incubated at room temperature for 30min. Get A Quote

摘要

Post-translational modification of ribosomal proteins enables rapid and dynamic regulation of protein biogenesis. Site-specific ubiquitylation of 40S ribosomal proteins uS10 and eS10 plays a key role during ribosome-associated quality control (RQC). Distinct, and previously functionally ambiguous, ubiquitylation events on the 40S proteins uS3 and uS5 are induced by diverse proteostasis stressors that impact translation activity. Here, we identify the ubiquitin ligase RNF10 and the deubiquitylating enzyme USP10 as the key enzymes that regulate uS3 and uS5 ubiquitylation. Prolonged uS3 and uS5 ubiquitylation results in 40S, but not 60S, ribosomal protein degradation in a manner independent of canonical autophagy.... More

关键词

RNF10, protein homeostasis, ribosome-associated quality control, translation initiation, ubiquitin
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