Proteostasis in eukaryotes is maintained by compartment-specific quality control 
pathways, which enable the refolding or the degradation of defective 
polypeptides to prevent the toxicity that may arise from their aggregation. 
Among these processes, translational protein quality control is performed by the 
Ribosome-bound Quality Control complex (RQC), which recognizes nascent peptides 
translated from aberrant mRNAs, polyubiquitylates these aberrant peptides, 
extracts them from the stalled 60S subunit and finally escorts them to the 
proteasome for degradation. In this review, we focus on the mechanism of action 
of the RQC complex from stalled 60S binding to aberrant peptide delivery to the 
proteasome and describe the cellular consequences of a deficiency in the RQC 
pathway, such as aberrant protein aggregation. In addition, this review covers 
the recent discoveries concerning the role of cytosolic chaperones, as well as 
Tom1, to prevent the accumulation of aberrant protein aggregates in case of a 
deficiency in the RQC pathway.