USP16 counteracts mono-ubiquitination of RPS27a and promotes maturation of the 40S ribosomal subunit

Open access
Date
2020Type
- Journal Article
Citations
Cited null times in
Web of Science
Cited 4 times in
Scopus
ETH Bibliography
yes
Altmetrics
Abstract
Establishment of translational competence represents a decisive cytoplasmic step in the biogenesis of 40S ribosomal subunits. This involves final 18S rRNA processing and release of residual biogenesis factors, including the protein kinase RIOK1. To identify novel proteins promoting the final maturation of human 40S subunits, we characterized pre-ribosomal subunits trapped on RIOK1 by mass spectrometry, and identified the deubiquitinase USP16 among the captured factors. We demonstrate that USP16 constitutes a component of late cytoplasmic pre-40S subunits that promotes the removal of ubiquitin from an internal lysine of ribosomal protein RPS27a/eS31. USP16 deletion leads to late 40S subunit maturation defects, manifesting in incomplete processing of 18S rRNA and retarded recycling of late-acting ribosome biogenesis factors, revealing an unexpected contribution of USP16 to the ultimate step of 40S synthesis. Finally, ubiquitination of RPS27a appears to depend on active translation, pointing at a potential connection between 40S maturation and protein synthesis. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000406660Publication status
publishedExternal links
Journal / series
eLifeVolume
Pages / Article No.
Publisher
eLife Sciences PublicationsOrganisational unit
03543 - Kutay, Ulrike / Kutay, Ulrike
03927 - Picotti, Paola / Picotti, Paola
Funding
166565 - Ribosome synthesis in mammalian cells (SNF)
More
Show all metadata
Citations
Cited null times in
Web of Science
Cited 4 times in
Scopus
ETH Bibliography
yes
Altmetrics