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Ubiquitylation by the Ltn1 E3 ligase protects 60S ribosomes from starvation-induced selective autophagy

Academic Article
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Overview

authors

  • Ossareh-Nazari, B.
  • Nino, C. A.
  • Bengtson, M. H.
  • Lee, J. W.
  • Joazeiro, Claudio Antonio
  • Dargemont, C.

publication date

  • March 2014

journal

  • Journal of Cell Biology  Journal

abstract

  • Autophagy, the process by which proteins or organelles are engulfed by autophagosomes and delivered for vacuolar/lysosomal degradation, is induced to ensure survival under starvation and other stresses. A selective autophagic pathway for 60S ribosomal subunits elicited by nitrogen starvation in yeast-ribophagy-was recently described and requires the Ubp3-Bre5 deubiquitylating enzyme. This discovery implied that an E3 ligases act upstream, whether inhibiting the process or providing an initial required signal. In this paper, we show that Ltn1/Rkr1, a 60S ribosome-associated E3 implicated in translational surveillance, acts as an inhibitor of 60S ribosomal subunit ribophagy and is antagonized by Ubp3. The ribosomal protein Rpl25 is a relevant target. Its ubiquitylation is Ltn1 dependent and Ubp3 reversed, and mutation of its ubiquitylation site rendered ribophagy less dependent on Ubp3. Consistently, the expression of Ltn1-but not Ubp3-rapidly decreased after starvation, presumably to allow ribophagy to proceed. Thus, Ltn1 and Ubp3-Bre5 likely contribute to adapt ribophagy activity to both nutrient supply and protein translation.

subject areas

  • Autophagy
  • Endopeptidases
  • Enzyme Repression
  • Gene Expression
  • Gene Expression Regulation, Fungal
  • Gene Knockout Techniques
  • Nitrogen
  • Ribosomal Proteins
  • Ribosome Subunits, Large, Eukaryotic
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Stress, Physiological
  • Ubiquitin-Protein Ligases
  • Ubiquitination
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Identity

PubMed Central ID

  • PMC3998797

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.201308139

PubMed ID

  • 24616224
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Additional Document Info

start page

  • 909

end page

  • 917

volume

  • 204

issue

  • 6

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