biostudies-literatureUnknown11(12)Kuroha KNascent peptide-dependent translation arrest is crucial for the quality control of eukaryotic gene expression. Here we show that the receptor for activated C kinase 1 (RACK1) participates in nascent peptide-dependent translation arrest, and that its binding to the 40S subunit is crucial for this. Translation arrest by a nascent peptide results in Dom34/Hbs1-independent endonucleolytic cleavage of mRNA, and this is stimulated by RACK1. We propose that RACK1 stimulates the translation arrest that is induced by basic amino-acid sequences that leads to endonucleolytic cleavage of the mRNA, as well as to co-translational protein degradation.EMBO reports956-61https://www.ebi.ac.uk/biostudies/studies/S-EPMC2999862biostudies-literatureReceptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest.PMC2999862Akamatsu MKato YShirahige KIto TDimitrova LInada TKuroha KfalseReceptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest.Nascent peptide-dependent translation arrest is crucial for the quality control of eukaryotic gene expression. Here we show that the receptor for activated C kinase 1 (RACK1) participates in nascent peptide-dependent translation arrest, and that its binding to the 40S subunit is crucial for this. Translation arrest by a nascent peptide results in Dom34/Hbs1-independent endonucleolytic cleavage of mRNA, and this is stimulated by RACK1. We propose that RACK1 stimulates the translation arrest that is induced by basic amino-acid sequences that leads to endonucleolytic cleavage of the mRNA, as well as to co-translational protein degradation.2010-01-01T00:00:00Z2010 Dec2025-04-05T14:46:04.361Z2019-03-27T00:37:17ZS-EPMC29998622107206310.1038/embor.2010.169