Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 47, Pages E7490-E7499Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1615455113
Keywords
proteasome; autophagy; ubiquitin; degradation
Categories
Funding
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- Israel Science Foundation (ISF)
- I-CORE Program of the Planning and Budgeting Committee
- ISF [1775/12]
- Deutsch-Israelische Projektkooperation
- Foulkes Fellowship
- special fund for research in the Technion
- National Research Foundation of Korea [2016R1A2B3011389] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The ubiquitin-proteasome system and autophagy are the two main proteolytic systems involved in, among other functions, the maintenance of cell integrity by eliminating misfolded and damaged proteins and organelles. Both systems remove their targets after their conjugation with ubiquitin. An interesting, yet incompletely understood problem relates to the fate of the components of the two systems. Here we provide evidence that amino acid starvation enhances polyubiquitination on specific sites of the proteasome, a modification essential for its targeting to the autophagic machinery. The uptake of the ubiquitinated proteasome is mediated by its interaction with the ubiquitin-associated domain of p62/SQSTM1, a process that also requires interaction with LC3. Importantly, deletion of the PB1 domain of p62, which is important for the targeting of ubiquitinated substrates to the proteasome, has no effect on stress-induced autophagy of this proteolytic machinery, suggesting that the domain of p62 that binds to the proteasome determines the function of p62 in either targeting substrates to the proteasome or targeting the proteasome to autophagy.
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