| Popis: |
During protein synthesis, organisms constantly survey defective translation events that may lead to ribosome stalling with consequent ribosome collisions. Translation problems can result in misfolded protein products that sequester ribosomes into intracellular protein aggregates. Cells have co-translational quality control mechanisms to eliminate these aberrant protein products before they are released from the ribosome. One of these mechanisms is the Ribosome-associated Quality Control (RQC) complex. To better understand the role of the RQC complex in mammals, we used public datasets of transcriptome and proteomics analysis to study the tissue distribution and profile of the three RQC components, namely, LTN1, TCF25, and NEMF, together with the ubiquitin ligase ZNF598, responsible for RQC recruitment. Our data shows that the RQC components are widely expressed in human tissues with no preference and their silencing lead to mild effects. Interestingly, TCF25 shows a particular profile with high mRNA levels that is not reflected in its protein content, suggesting a post-translational regulation. Finally, cellular aging caused a mild impact on their expression, causing a decrease in mRNA levels in some human tissues. Our data suggest that the RQC is essential in maintaining proteostasis in all mammalian tissues but is not vital for cell survival. |
