Protein Stability Buffers the Cost of Translation Attenuation following eIF2α Phosphorylation.

ABSTRACT: Phosphorylation of the translation initiation factor eIF2α is a rapid and vital response to many forms of stress, including protein-misfolding stress in the endoplasmic reticulum (ER stress). It is believed to cause a general reduction in protein synthesis while enabling translation of few transcripts. Such a reduction of protein synthesis comes with the threat of depleting essential proteins, a risk thought to be mitigated by its transient nature. Here, we find that translation attenuation is not uniform, with cytosolic and mitochondrial ribosomal subunits being prominently downregulated. Translation attenuation of these targets persists after translation recovery. Surprisingly, this occurs without a measurable decrease in ribosomal proteins. Explaining this conundrum, translation attenua

SUBMITTER: Schneider K 

PROVIDER: S-EPMC7495045 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature