Systematic quantitative analysis of ribosome inventory during nutrient stress.

ABSTRACT: Mammalian cells reorganize their proteomes in response to nutrient stress through translational suppression and degradative mechanisms using the proteasome and autophagy systems^1,2. Ribosomes are central targets of this response, as they are responsible for translation and subject to lysosomal turnover during nutrient stress^3-5. The abundance of ribosomal (r)-proteins (around 6% of the proteome; 10⁷ copies per cell)^6,7 and their high arginine and lysine content has led to the hypothesis that they are selectively used as a source of basic amino acids during nutrient stress through autophagy^4,7. However, the relative contributions of translational and degradative mechanisms to the control of r-protein abundance during acute stress respon

SUBMITTER: An H 

PROVIDER: S-EPMC7351614 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature