Amino-terminal arginylation as a degradation signal for selective autophagy

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Title
Amino-terminal arginylation as a degradation signal for selective autophagy
Author(s)
Hyunjoo Cha; Y T Kwon; Bo Yeon Kim
Bibliographic Citation
BMB Reports, vol. 48, no. 9, pp. 487-488
Publication Year
2015
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.
Keyword
ATE1Autophagyp62
ISSN
1225-8687
Publisher
South Korea
DOI
http://dx.doi.org/10.5483/BMBRep.2015.48.9.176
Type
Article
Appears in Collections:
Ochang Branch Institute > Anticancer Agent Research Center > 1. Journal Articles
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