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Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest.

ABSTRACT: 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.

SUBMITTER: Kuroha K

PROVIDER: S-EPMC2999862 | biostudies-other | 2010 Dec

REPOSITORIES: biostudies-other

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Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest.

Kuroha Kazushige K Akamatsu Mayuko M Dimitrova Lyudmila L Ito Takehiko T Kato Yuki Y Shirahige Katsuhiko K Inada Toshifumi T

EMBO reports 20101112 12

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 ...[more]

PMID: 21072063

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