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Yeast extracts recapitulate a quality-control pathway dedicated to rescuing stalled ribosomes, providing unexpected insights into a noncanonical elongation reaction and the fate of incompletely synthesized proteins.

Alkylation stress modify mRNAs and results in translation arrest, which activates the ribosome-rescue pathway of trans translation in bacteria.

The deubiquitinase USP16 is associated with cytoplasmic precursors of 40S ribosomal subunits and promotes their final maturation by removal of trans-monoubiquitin from RPS27a.

The enzyme that collaborates with ubiquitin ligases to promote the release of defective polypeptides from stalled ribosomes in a process named ribosome-associated degradations has been identified as the ATPase Cdc48.

A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.

Cue2 is an endonuclease that cleaves mRNA in the A site of the lagging ribosome upon ribosome collision events.

Cryo-EM reveals how the central functional site of the ribosome is assembled and provides a framework to interpret the consequences of mutations linked to leukaemia-associated ribosomopathies.

The translational GTPase GTPBP1 prevents ribosome stalling during tRNA deficiency and is necessary for neuronal survival.

Disruption of quality control pathways that function at distinct steps to mitigate errors in translation evoke similar cellular responses and pathologies.

Removal of spurious poly(A) tails by the PDE12 exoribonuclease is required to maintain the integrity of human mitochondrial tRNAs and rRNAs and their availability for efficient mitochondrial translation.