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Amino-terminal arginylation as a degradation signal for selective autophagy
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  • Journal title : BMB Reports
  • Volume 48, Issue 9,  2015, pp.487-488
  • Publisher : Korean Society for Biochemistry and Molecular Biology
  • DOI : 10.5483/BMBRep.2015.48.9.176
 Title & Authors
Amino-terminal arginylation as a degradation signal for selective autophagy
Cha-Molstad, Hyunjoo; Kwon, Yong Tae; Kim, Bo Yeon;
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 Abstract
The ubiquitin-proteasome system and the autophagy lysosome system are the two major protein degradation machineries in eukaryotic cells. These two systems coordinate the removal of unwanted intracellular materials, but the mechanism by which they achieve this synchronization is largely unknown. The ubiquitination of substrates serves as a universal degradation signal for both systems. Our study revealed that the amino-terminal Arg, a canonical N-degron in the ubiquitin-proteasome system, also acts as a degradation signal in autophagy. We showed that many ER residents, such as BiP, contain evolutionally conserved arginylation permissive pro-N-degrons, and that certain inducers like dsDNA or proteasome inhibitors cause their translocation into the cytoplasm where they bind misfolded proteins and undergo amino-terminal arginylation by arginyl transferase 1 (ATE1). The amino-terminal Arg of BiP binds p62, which triggers p62 oligomerization and enhances p62-LC3 interaction, thereby stimulating autophagic delivery and degradation of misfolded proteins, promoting cell survival. This study reveals a novel ubiquitin-independent mechanism for the selective autophagy pathway, and provides an insight into how these two major protein degradation pathways communicate in cells to dispose the unwanted proteins. [BMB Reports 2015; 48(9): 487-488]
 Keywords
ATE1;p62;Autophagy;
 Language
English
 Cited by
1.
Structure biology of selective autophagy receptors, BMB Reports , 2016, 49, 2, 73  crossref(new windwow)
2.
Autophagy-Related Deubiquitinating Enzymes Involved in Health and Disease, Cells, 2015, 4, 4, 596  crossref(new windwow)
3.
Titin, a Central Mediator for Hypertrophic Signaling, Exercise-Induced Mechanosignaling and Skeletal Muscle Remodeling, Frontiers in Physiology, 2016, 7  crossref(new windwow)