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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Mario H. Bengtson & Claudio A. P. Joazeiro, 2010. "Role of a ribosome-associated E3 ubiquitin ligase in protein quality control," Nature, Nature, vol. 467(7314), pages 470-473, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7314:d:10.1038_nature09371
    DOI: 10.1038/nature09371
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    Cited by:

    1. Joana Silva & Ferhat Alkan & Sofia Ramalho & Goda Snieckute & Stefan Prekovic & Ana Krotenberg Garcia & Santiago Hernández-Pérez & Rob Kammen & Danielle Barnum & Liesbeth Hoekman & Maarten Altelaar & , 2022. "Ribosome impairment regulates intestinal stem cell identity via ZAKɑ activation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Ken Ikeuchi & Nives Ivic & Robert Buschauer & Jingdong Cheng & Thomas Fröhlich & Yoshitaka Matsuo & Otto Berninghausen & Toshifumi Inada & Thomas Becker & Roland Beckmann, 2023. "Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Yoshitaka Matsuo & Takayuki Uchihashi & Toshifumi Inada, 2023. "Decoding of the ubiquitin code for clearance of colliding ribosomes by the RQT complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Katharina Best & Ken Ikeuchi & Lukas Kater & Daniel Best & Joanna Musial & Yoshitaka Matsuo & Otto Berninghausen & Thomas Becker & Toshifumi Inada & Roland Beckmann, 2023. "Structural basis for clearing of ribosome collisions by the RQT complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    5. Jiangnan Liu & Noemi Nagy & Carlos Ayala-Torres & Francisco Aguilar-Alonso & Francisco Morais-Esteves & Shanshan Xu & Maria G. Masucci, 2023. "Remodeling of the ribosomal quality control and integrated stress response by viral ubiquitin deconjugases," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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