Role of a ribosome-associated E3 ubiquitin ligase in protein quality control

Mario H. Bengtson and Claudio A. P. Joazeiro ()
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Mario H. Bengtson: The Scripps Research Institute, CB168, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Claudio A. P. Joazeiro: The Scripps Research Institute, CB168, 10550 North Torrey Pines Road, La Jolla, California 92037, USA

Nature, 2010, vol. 467, issue 7314, 470-473

Abstract: Protein quality control Translation of mRNAs lacking stop codons (nonstop mRNA) results in the production of aberrant proteins that may have deleterious effects on cellular function. It is unclear how eukaryotic cells eliminate such 'nonstop' proteins. In this study, Mario Bengtson and Claudio Joazeiro demonstrate that in the yeast Saccharomyces cerevisiae, an E3 ubiquitin ligase called Ltn1 acts in the quality control pathway. It associates with ribosomes and marks nonstop proteins that are then targeted for proteasomal degradation by the ubiquitin pathway. Ltn1-mediated ubiquitylation is triggered when the proteins stall at the poly(A) tail in the ribosomes on translation. Loss of Ltn1 function conferred increased cellular stress as a result of elevated levels of nonstop proteins.

Date: 2010
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DOI: 10.1038/nature09371

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