Accumulation of impaired proteins poses a critical issue for all cells, and elaborate quality control systems have evolved to minimize their effects. In particular, cells have developed failsafe mechanisms to cope with deleterious ribosomal stalls that result from damaged mRNA. Though temporary ribosome stalls can have biological functions, like co-translational protein folding or targeting, persistent stalls are generally indicative of a stress, leading to ribosomal collisions, promoting degradation of the nascent peptide (NP) and triggering mRNA decay. Recognition of ribosomal collisions involves factors and mechanisms that are highly conserved in eukaryotes, as exemplified in the S. cerevisiae model. Thus, ribosome collisions form a particular conformation recognized by a conserved ubiquitin ligase, Hel2. Specific ribosomal proteins are then ubiquitinated and associate with the Ribosome Quality Triggering (RQT) complex, which disassembles the colliding ribosomes and generates a 60S subunit still attached to a peptidyl RNA. Then, the Ribosome-mediated Quality Control (RQC) pathway can interact with this particular 60S subunit, and triggers the degradation of the arrested product by the proteasome system. It is proposed that this quality control is coupled to mRNA decay processes that target problematic mRNAs and prevent ribosomes from continuously producing aberrant peptides, potentially toxic to the cell. It is now admitted that problematic mRNAs (stalling within coding sequence) are mostly degraded through 5’-decapping and 5’-3’ exonucleolytic processing by the canonical degradation machinery, with the 5’-3’ exoribonuclease Xrn1 playing a major role. How all these processes are coordinated has not been clarified. Nor has the interconnection of these processes been elucidated, if it exists at all. To investigate whether mRNA and peptide degradation are coupled, we wondered whether mRNA decay factors are able to affect RQT and/or RQC processes. We thus designed different mRNA reporters containing rare codons, and analyzed the impact of a set of mRNA decay mutants on aberrant peptide production. The tricky part of this approach is that a greater stabilization of faulty mRNAs may simply result, in a passive mode, in the accumulation of aberrant peptides. We have therefore designed our mRNA reporters to limit this issue and we propose promising candidates interconnecting all these quality control processes via mechanisms and interactions to be deciphered.