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Mol Cell Biol. 2013 Jul;33(13):2510-26. doi: 10.1128/MCB.01362-12. Epub 2013 Apr 22.

Degradation of newly synthesized polypeptides by ribosome-associated RACK1/c-Jun N-terminal kinase/eukaryotic elongation factor 1A2 complex.

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1
Department of Biochemistry and Goodman Cancer Centre, McGill University, Montréal, Québec, Canada.

Abstract

Folding of newly synthesized polypeptides (NSPs) into functional proteins is a highly regulated process. Rigorous quality control ensures that NSPs attain their native fold during or shortly after completion of translation. Nonetheless, signaling pathways that govern the degradation of NSPs in mammals remain elusive. We demonstrate that the stress-induced c-Jun N-terminal kinase (JNK) is recruited to ribosomes by the receptor for activated protein C kinase 1 (RACK1). RACK1 is an integral component of the 40S ribosome and an adaptor for protein kinases. Ribosome-associated JNK phosphorylates the eukaryotic translation elongation factor 1A isoform 2 (eEF1A2) on serines 205 and 358 to promote degradation of NSPs by the proteasome. These findings establish a role for a RACK1/JNK/eEF1A2 complex in the quality control of NSPs in response to stress.

PMID:
23608534
PMCID:
PMC3700114
DOI:
10.1128/MCB.01362-12
[Indexed for MEDLINE]
Free PMC Article
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